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Volume 74 (1973)
- Issue 6 Pages 1075-
- Issue 5 Pages 863-
- Issue 4 Pages 639-
- Issue 3 Pages 405-
- Issue 2 Pages 203-
- Issue 1 Pages 1-
Volume 74, Issue 3
Displaying 1-28 of 28 articles from this issue
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Yoshiko KASHIWABARA, Ryo SATO1973 Volume 74 Issue 3 Pages 405-413
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe particulate fraction prepared from sonic extracts of Mycobacterium phlei catalyzes the desaturation of stearoyl-CoA in the presence of molecular oxygen, NADPH, and exogenous FAD; no requirement for ferrous ion is, however, detectable. Like the similar desaturase system of rat liver microsomes, the M. phlei system appears to contain a cyanide-sensitive factor as the terminal enzyme. Two types of NADPH-cytochrome c reductase activity are detectable in the particulate fraction; one is a weak activity which is independent of exogenous FAD and the other requires added FAD for activity. Similarities between the behavior of the FAD-requiring cytochrome c reductase activity and that of the overall desaturase activity toward KCl, HgCl2, Emalgen 911, etc. indicate the participation of this reductase activity in the desaturation system. The NADPH-ferricyanide reductase activity of the particulate fraction is not enhanced by exogenous FAD and its properties differ from those of the FAD-requiring NADPH-cytochrome c reductase activity in several respects. The soluble fraction of M. phlei also contains an FAD-requiring NADPH-cytochrome c reductase activity, but its properties are again different from those of its particulate counterpart. Based on these findings, the electron transfer mechanism involved in the stearoyl-CoA desaturase system of M. phlei is discussed.View full abstractDownload PDF (771K) -
Yoshiki TAKESUE, Takato O. YOSHIDA, Tatsuya AKAZA, Yoshimi NISHI1973 Volume 74 Issue 3 Pages 415-423
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSRabbit intestinal sucrase [EC 3. 2. 1] was purified by solubilization with papain or Triton X-100 followed by adsorption on Sephadex G-200 gel. Antibodies were developed in a goat against purified papain-solubilized sucrase and in guinea pigs against purified Triton-solubilized sucrase. Both antibodies precipitated microvillous membrane-bound sucrase and other hydrolases in a parallel manner, but did not precipitate solubilized hydrolases except sucrase, indicating that these microvillous hydrolases were located very close to each other and scattered on the microvillous membrane. The antibody to Triton-solubilized sucrase contained an antibody species which was not absorbed by microvillous membranes; it precipitated Triton-solubilized sucrase but not papain-solubilized sucrase. This same antibody species was not found in anti-papain-solubilized sucrase antibody. On the basis of these findings the state of sucrase molecules anchored in the microvillous membrane is discussed.View full abstractDownload PDF (1643K) -
Susumu YASUOKA, Setsuro FUJII, Toshijiro YAMAGUCHI, Katsukiyo SAKURAI, ...1973 Volume 74 Issue 3 Pages 425-434
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSUsing synthetic sulfated polysaccharides (SP's) of relatively low molecular weight, the effects of SP's on lipoprotein lipase [EC 3. 1. 1. 3] (LPL) were examined.
(1) The activities of synthetic SP's in the liberation of LPL are proportional to their activities for the inhibition of the LPL activity.
(2) The activities of these SP's in the liberation of LPL both in vivo and in vitro, and for the inhibition of the LPL activity are proportional to their sulfate contents and molecular weights.
(3) The chemical nature of the repeating a sugar units and the type of glycosidic linkage in synthetic SP's do not appreciably influence their activities in the liberation of LPL or for the inhibition of the LPL activity.
(4) Unlike synthetic SP's, heparin has a specific effect on the liberation of LPL only in vivo.
(5) The release of LPL from adipose tissue in vitro increases with increase in the ionic strength of the incubation medium.
(6) The mechanism whereby SP's liberate LPL into the blood stream is discussed on the basis of these results.View full abstractDownload PDF (706K) -
Hirofumi ONISHI, Eiko OHTSUKA, Morio IKEHARA, Yuji TONOMURA1973 Volume 74 Issue 3 Pages 435-450
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The hydrolysis of 1, N6-ethenoadenosine triphosphate (εATP) by myosin [EC 3. 6. 1. 3] and the change in fluorescence of εATP induced by H-meromyosin were studied.
(a) The amount of initial burst (TCA-labile Pi formation) of εATP-splitting was 1.1-1.3 moles per mole (4.8×105g) of myosin. In the steady-state of the myosin-εATPase reaction, the maximum rate and the Michaelis-Menten constant were 0.13 sec-1 and 0.93μM, respectively.
(b) The excitation spectrum of the 410nm fluorescence of εATP was changed upon addition of H-meromyosin; the fluorescence intensity decreased in the 310nm region and increased in the 290nm region.
(c) Both the decrease and the increase in the fluorescence followed the same timecourse, including the recovery to the initial intensity. The rate of the change (either increase or decrease) in the εATP fluorescence was measured. The results obtained can be treated by using the Michaelis-Menten equation. The maximum rate and Michaelis-Menten constant were 7.4sec-1 and 36μM, respectively. The rate in the recovery phase was 0.1sec-1.
(d) The reaction steps and the assignment of the kinetic parameters obtained above are proposed to be as follows:
_??_.
Here, ES stands for a enzyme-substrate complex, and EεADPP for the myosin-phosphate-εADP complex, the formation of which accompanies the fluorescence change of εATP. The assignment of the parameters (0.13sec-1 and 0.93 μM) obtained for the phosphate liberation in the steady-state was unsettled at present.
2. The interaction of H-meromyosin and εATP was studied by measuring the difference absorption spectrum, the difference fluorescence emission spectrum and the iodide-quenching of fluorescence.
(a) The difference absorption spectrum of H-meromyosin induced by εATP was similar to that induced by ATP, but the former was about 80% of the latter in the magnitude.
(b) When excited at 288nm, the emission spectrum of the reaction mixture (εATP plus H-meromyosin) showed a decreased intensity in the 340nm region and an increased intensity in the 410nm region.
(c) Judging from the portion of fluorescence intensity at 340nm that was not quenched by KI, the amount of tryptophan residues of H-meromyosin “inaccessible” to iodide was increased by adding εATP. This increase is approximately 80% of the increase obtained with ATP.
(d) A quantitative comparison between the increase at 410nm and the decrease at 340nm indicated that the transfer of excitation energy occurs only from “accessible” (to iodide) tryptophan residues to the εATP bound to H-meromyosin.View full abstractDownload PDF (1121K) -
Kiyoshi FURUICHI, Takayuki SASAKI, Jiro KOYAMA1973 Volume 74 Issue 3 Pages 451-457
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSAdenosine 5'-phosphate (AMP)** specific IgM and IgG antibodies were obtained by immunization of rabbits with an AMP-E. coli conjugate prepared by coupling periodate-oxidized AMP with the cells. The antibodies were purified using an AMP-ovalbumin (AMP-OA)-agarose conjugate as immunoadsorbent. IgM antibody was separated from IgG antibody by gel-filtration with Sephadex G-200. Relatively large amounts of IgM antibody were separated from the early immune sera. Both the IgM and IgG antibodies showed complement fixing reactions with heat-denatured deoxynucleic acid (d-DNA), but markedly weak reactions with native DNA. The hapten inhibition technique revealed that specificity of these antibodies was directed toward AMP, and in particular, adenine base.View full abstractDownload PDF (584K) -
Fumio SAWADA, Noriko KANBAYASHI1973 Volume 74 Issue 3 Pages 459-471
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSBovine pancreatic ribonuclease A [EC 2. 7. 7. 16] was inactivated by irradiation with near-ultraviolet light in the presence of 4-thiouridylic acid (F. Sawada, J. Biochem., 65, 767 (1969)). The irradiated enzyme was fractionated into two classes: partially inactivated monomers and inactivated aggregates.
The monomers were composed of at least 6 components. It seemed that cystinyl residues in the protein participated in the photochemical modification which resulted in the formation of new disulfide bonds between the cysteinyl residues and thiouridylic acid or its photoproducts. In addition, photooxidation at methionyl residues in the protein was suggested.
The major portion of the aggregates was found to represent dimers on the basis of molecular weight determinations by gel filtration and SDS-gel electrophoresis. They were fractionated into 3 fractions. (1) Aggregates dissociable by denaturation which were formed by non-covalent interactions. (2) Aggregates dissociable by reduction which were formed presumably by disulfide interchanges between the two monomer molecules. (3) Aggregates undissociable by both denaturation and reduction of which chemical natures are unknown.View full abstractDownload PDF (2438K) -
II. Slvent Perturbation Spectroscopy of Ferricytochrome aTakashi YAMAMOTO, Yutaka ORII1973 Volume 74 Issue 3 Pages 473-479
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe location of heme a in ferricytochrome a (cytochrome oxidase [EC 1. 9. 3. 1]) was studied by the solvent perturbation technique. The heme a in a cytochrome a molecule was found to come into contact with methanol to a considerable extent but only to a very small extent with ethylene glycol and glycerol, although the latter two compounds appreciably affected free heme a in aqueous Emasol. These results suggest that the heme a in ferricytochrome a is almost buried in the molecule, with the formyl side group being exposed to a perturbing solvent of a high hydrogendonating capacity.View full abstractDownload PDF (1461K) -
Kiyoshi SHIGA, Akio ISOMOTO, Kihachiro HORIIKE, Toshio YAMANO1973 Volume 74 Issue 3 Pages 481-488
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSBy analyzing the reaction of D-amino-acid oxidase [EC 1. 4. 3. 3] in equilibrium with p-aminobenzoate, we studied the functional difference between the affinities of the monomer and the dimer for p-aminobenzoate, the interaction between the two active sites in the dimer (i.e., cooperativity), and the shift in the equilibrium between monomer and dimer induced by p-aminobenzoate.
We found that the affinity of the dimer for p-aminobenzoate is about five times higher than that of the monomer, and there is no interaction between the two active sites in the dimer (i.e., no cooperativity). Based on our findings, we concluded that p-aminobenzoate induces dimerization of D-amino-acid oxidase. The apparent dimerization constant in the presence of an infinite concentration of p-aminobenzoate is about 20 times greater than in its absence. The apparent dimerization constant was calculated as a function of the concentration of free p-aminobenzoate, using a Hitachi Hitac-10 digital computer. The relationship is not hyperbolic, but has a point of inflection.View full abstractDownload PDF (603K) -
Keiko KUROZUMI, Teruo HARANO, Kazumi YAMASAKI, Yoshikazu AYAKI1973 Volume 74 Issue 3 Pages 489-495
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe following 5 samples of bear bile were analyzed: two Japanese bear bites, JBB1 and JBB2; three Himalayan bear bites, HBB, FUt, and FUm. Two types, A and B, of bile acid pattern were found in these samples: Type A-The major acid was cholic acid, inclusive of its secondary acid (deoxycholic acid) (JBB1, JBB2, and FUt); type B-The major acid was ursodeoxycholic acid, inclusive of its primary acid (chenodeoxycholic acid) (HBB and FUm). This finding might constitute a taxonomically significant criterion among the species of Ursidae.
The total concentration of bile acids was found to be high in samples JBB2, HBB, FUt, and FUm, whereas that of sample JBB1 was very low. Concentration differences in total bile acids were discussed in relation to the length of the hibernation (fasting) period of the species of Ursidae.View full abstractDownload PDF (470K) -
Glorietta P. VIDAL, Makoto SASAKI1973 Volume 74 Issue 3 Pages 497-503
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSFruit bromelain [EC 3. 4. 4. 24] cleaved human IgG into two kinds of fragments separable by CM- and DEAF-cellulose column chromatography. The resulting fragments, Fab(F) and Fc(F), apparently resembled those obtained using papain [EC 3. 4. 4. 10] as regards antigenicity, electrophoretic mobility, sedimentation constant, molecular weight, and amino acid composition. Fab(F) and Fc(F) had sedimentation constants of 3.7S and 3.5S, respectively. Fab(F) was shown by gel filtration to have a molecular weight of 51, 000 and Fc(F) a molecular weight of 48, 000. These results suggest that the possible site of fruit bromelain cleavage of human IgG could be very close to that of papain.
Studies of the cleavage by fruit bromelain of human IgG at different enzymesubstrate ratios and digestion times showed that human IgG has a stronger resistance to fruit bromelain than to papain. By experiments on subclass specificity, it was shown that this difference in resistance to enzymatic attack was mainly due to the difference in the nature of the enzyme-resistant subclass. Thus, the fruit bromelainresistant component involves IgG 1 and IgG 2, whereas it has been shown that the papain-resistant component involves only IgG 2.View full abstractDownload PDF (1405K) -
Eisuke HANADA, F. K. ANAN1973 Volume 74 Issue 3 Pages 505-511
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe insoluble collagen fraction (ICF) was prepared from bovine nasal cartilage by aqueous extraction (Schubert's method), followed by extraction with 8M urea in 1M NaCl. The amino acid composition of the ICF was very similar to that of the soluble cartilage collagen ever reported, but the ICF contained small amounts of hexuronic acid, hexose, hexosamine, and sialic acid. The ICF in the particle form was shown to bind chondroitin sulfate C (ChS-C) at pH 3.40, and to a lesser extent, at pH 7.30. The similar binding of cartilage acid glycosaminoglycan and proteoglycan with ICF was also demonstrated. An ICF column which adsorbed ChS-C at pH 3.40 exhibited one peak by pH gradient elution between pH 3.40 and 7.30, and another peak by NaCI gradient (0→1.0M) elution at pH 7.30.View full abstractDownload PDF (584K) -
Yozo TAKASAKI, Kazutomo IMAHORI1973 Volume 74 Issue 3 Pages 513-517
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSWe found that Y base from tRNAPhe showed a positive CD peak at 327nm, and that its intensity varied in accordance with the concentration of Mg2+ or spermidine. Similar changes were observed in the fluorescence spectra and it was deduced that such changes are due to a conformational change probably in the region of the anticodon loop. CD and fluorescence spectra of phenylalanyl-tRNAPhe were also measured and the conformational change of tRNA accompanying amino-acylation was discussed. The apparent binding constant of phenylalanyl-tRNAPhe with poly U was estimated to be 4.4×103M-1 by the fluorescence technique.View full abstractDownload PDF (344K) -
Masatake OHNISHI, Hiroyuki HATANO, Keitaro HIROMI1973 Volume 74 Issue 3 Pages 519-524
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe number of exposed tryptophan residues in bacterial saccharifying α-amylase was estimated by the solvent perturbation technique using several perturbants. Five to six of the eleven residues were found to be exposed.
A difference spectrum of the enzyme, attributable to one tryptophan residue, was found to be produced by addition of cycloheptaamylose.
The Michaelis constant, Km and the molecular activity, k0 for hydrolysis of cycloheptaamylose by the enzyme were determined at pH 5.4 and 25°C. The Km value is slightly larger than that for maltotriose but considerably smaller than that for maltose, suggesting that the binding of cycloheptaamylose involves nearly three subsites.
These results indicate that one of the five to six exposed tryptophan residues of the enzyme is located in one of the three subsites and is responsible for the difference spectrum produced upon binding of cycloheptaamylose.View full abstractDownload PDF (439K) -
Yusuke MIZUNO, Michitomo YAEGASHI, Eiji ITO1973 Volume 74 Issue 3 Pages 525-538
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe enzyme which catalyzes the adenosine triphosphate-dependent addition of L-alanine to uridine diphosphate N-acetylmuramic acid has been purified approximately 100-fold from Staphylococcus aureus. The products of the reaction are uridine diphosphate N-acetylmuramyl-L-alanine, adenosine diphosphate, and inorganic phosphate. In addition to glycine, DL-serine at high concentrations acts as substrate, but D-alanine does not. The enzyme reaction requires NH4+ or K+ besides Mn2+ or Mg2+ and is stimulated markedly by 2-mercaptoethanol.View full abstractDownload PDF (2752K) -
Shoichi NAKASHIMA, Masanori MAZAKI, Kazuhisa SUGIMURA1973 Volume 74 Issue 3 Pages 539-544
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSSpecific anti-4-azoquinoline 1-oxide antibodies were prepared by the use of immunoadsorbent. The average association constants with 14C-4-nitroquinoline 1-oxide (4NQO) were in the range of 1-2×105L/M. The relative affinities for 4-aminoquinoline 1-oxide (4AQO) and 4-aminoquinoline (4AQ) were 0.061 and 0.024, respectively, taking that of 4NQO as 1.
It is suggested that the anti-hapten antibody-Chromagel conjugates might serve as a means for the isolation of some cross-reacting metabolites of 4NQO.View full abstractDownload PDF (491K) -
Yutaka UDA, Yasuo NAKAZAWA1973 Volume 74 Issue 3 Pages 545-549
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Proteolipid prepared from bovine brain was treated with ethanol-ether to remove the sphingomyelin component, and the remaining portion was dialyzed against chloroform-methanol. The undialyzable fraction consisted of 15% phospholipid and 3% glycolipid in addition to a proteinous component.
2. The phospholipid in the undialyzable fraction was composed mainly of acidic phospholipid. The amount was estimated to be equivalent to about 30% of the total basic amino acid content in the protein moiety.
3. Most of the acidic phospholipid in the undialyzable fraction could be removed by further dialysis against acidic chloroform-methanol.
4. The data presented suggest a stoichiometric relationship between acidic phospholipid and protein, bound by electrostatic forces in the proteolipid.View full abstractDownload PDF (360K) -
Yukiko TOKUMITSU, Michio UI1973 Volume 74 Issue 3 Pages 551-560
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe results of 32Pi-labelling of the organic phosphate fraction in rat-liver mitochondria incubated in ATP- (or ADP-) free media have been compared with those of 32Pi-labelling in media with ATP (or ADP) added. Differences have been noted in the sensitivity to uncouplers and inhibitors of oxidative phosphorylation, in the pH-activity profile, in the Arrhenius plot and in the 32P distribution among nucleotides. In the case of phosphorylation in the ATP- (or ADP-) free medium, significant generation of 32P-ADP is further enhanced by uncouplers, counterbalancing the uncoupler-induced inhibition of 32P-ATP formation and thus causing the 32P-labelling of the whole organic phosphate fraction to be apparently insensitive to the uncoupler. This forms a sharp contrast with the phosphorylation pattern observed in media with ATP (or ADP) added, in which there is an almost exclusive labelling of the ATP fraction. Electron acceptors, like uncouplers, increase 32Pi incorporation into ADP. The oxidation of glutamate as well as the regeneration of NAD+ from NADH is also accelerated by uncouplers and electron acceptors under exactly the same conditions.
Together with the previous conclusion that the incorporation of 32Pi into ADP inside the inner membrane is closely connected with 2-oxoglutarate-linked substratelevel phosphorylation, these findings indicate that the regeneration of NAD+ caused by the transfer of electrons across the respiratory chain plays a significant role in controlling the citric acid cycle as well as coupled substrate-level phoslhorylation.View full abstractDownload PDF (731K) -
Yukiko TOKUMITSU, Michio UI1973 Volume 74 Issue 3 Pages 561-572
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSMitochondrial preparations incubated with 32Pi and 3H-ADP were subjected to rapid filtration through a Millipore filter to study the intramitochondrial distribution of labelled nucleotides. The atractyloside-induced inhibition of the distribution of internally-labelled nucleotides and of externally-added 3H-ADP revealed that the nucleotides in the matrix space are successfully separated by this means from those outside the inner membrane. The addition of Mg2+ to the incubation medium has no effect on the labelling pattern in the matrix space but results in a rapid interconversion of adenine nucleotides outside the inner membrane through the activation of adenylate kinase [EC 2. 7. 4. 3] and nucleosidediphosphate kinase [EC 2. 7. 4. 6], which do not function in an Mg2+-free medium. The localization of GTP-AMP phosphotransferase [EC 2. 7. 4. 10] outside the membrane is questionable, but was not definitely excluded.
The translocation of internal ATP outwards in exchange for external ATP or ADP induced by the addition of ATP or ADP, of hexokinase plus glucose or of myokinase (muscle adenylate kinase) plus AMP into the incubation medium appears to be a significant factor in promoting the labelling of ATP, reflecting oxidative phosphorylation. 32Pi Labelling of ADP dependent on substrate-level phosphorylation is greatly suppressed under these conditions. This apparent suppression of substrate-level phosphorylation is at least partly accounted for in terms of the lowered specific radioactivity of the Pi compartment selectively supporting AMP phosphorylation as compared to the specific radioactivity of the major Pi pool serving as the substrate for oxidative phosphorylation. A possible interaction of these two phosphorylation reactions in rat-liver mitochondria is also discussed.View full abstractDownload PDF (938K) -
Katsuhide YUTANI, Ikuharu SASAKI, Kyoko OGASAHARA1973 Volume 74 Issue 3 Pages 573-579
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1) α-Amylases [EC 3. 2. 1. 1] from B. stearothermophilus grown at 55°C were separated into two isozymes by chromatography on DEAE-cellulose. The major component showed greater thermostability than the minor one.
2) The properties of the two isozymes were compared with those of an α-amylase from the same bacterium grown at 43°C. The α-amylase produced at 43°C was similar to the major component of the α-amylases produced at 55°C as regards various properties such as molecular weight, amino acid composition, electrophoretic properties, enzymatic properties, thermostability, and the pattern of circular dichroism.
3) The minor component produced at 55°C was probably not a proteolytic product derived from the major component during culture or purification.View full abstractDownload PDF (1468K) -
Katsuhide YUTANI1973 Volume 74 Issue 3 Pages 581-586
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe molecular weights of two α-amylase isozymes [EC 3. 2. 1. 1] (55°C α-amylases I and II) from B. stearothermophilus grown at 55°C and α-amylase [EC 3. 2. 1. 1] (43°C α-amylase) from the same bacterium grown at 43°C were determined by different methods (gel filtration and sedimentation equilibrium). The α-amylase produced at 43°C contained both monomeric and dimeric forms of the enzyme. To elucidate the effects arising from dimerization, the enzymes were reduced and carboxymethylated and then the molecular weight was measured in 6.1M guanidine hydrochloride solution. The molecular weights of 43°C α-amylase and 55°C α-amylases I and II were determined by sedimentation equilibrim to be 44, 000, 46, 000, and 43, 000 and by gel filtration (Sepharose 6B) to be 41, 000, 44, 000, and 41, 000, respectively.View full abstractDownload PDF (437K) -
Ikuko TOMONO, Miyako ABE, Makoto MATSUDA1973 Volume 74 Issue 3 Pages 587-592
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe effect of penicillamine administration on pyridoxal enzyme activities of rats was investigated. Penicillamine reduced the activities of glutamate decarboxylase [EC 4. 1. 1. 15] in brain and ornithine aminotransferase [EC 2. 6. 1. 13] in small intestine, and increased those of ornithine and tyrosine aminotransferases [EC 2. 6. 1. 5] in liver. It did not cause much change in the activities of kidney ornithine aminotransferase or liver aspartate or alanine aminotransferases [EC 2. 6. 1. 1 and 2]. Changes in these activities were prevented by simultaneous injection of pyridoxine. A marked increase in activity of the inactivating enzyme for pyridoxal enzymes was also observed in the small intestine of animals treated with penicillamine. Treatment of adrenalectomized rats with penicillamine unaffected liver ornithine aminotransferase activity. The possible interrelation between penicillamine and these pyridoxal enzymes is discussed in this paper.View full abstractDownload PDF (447K) -
Comparison of the Compositions of Different Fractions of Hog Thyroglobulin and of Thyroglobulins from Various Animal SpeciesNobuo UI1973 Volume 74 Issue 3 Pages 593-599
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe composition of neutral and amino sugars in different preparations of hog thyroglobulin and in thyroglobulins obtained from various animal species, i.e., amphibia (Xenopus laevis), ayes (chicken), and mammals (whale, monkey, and human) was determined. In determining neutral sugar compositions, gas-liquid chromatography of the alditol acetates was performed, while amino sugars were analyzed by ionexchange chromatography.
1. All the thyroglobulins studied were glycoproteins containing both neutral and amino sugars. Fucose, mannose, galactose, and glucosamine were common constituent sugars, and a small amount of galactosamine was found in thyroglobulins other than hog and Xenopus laevis.
2. Different subfractions of hog thyroglobulin obtained by DEAE-cellulose chromatography and a preparation of noniodinated thyroglobulin prepared from goitrogentreated hog showed essentially the same composition of neutral and amino sugars, irrespective of the large differences in iodine content. A slightly different composition was observed with one minor subfraction only, in which the mannose and glucosamine contents were somewhat lower than those of other subfractions, and noniodinated hog thyroglobulin contained a slightly lower amount of glucosamine than normally iodinated hog thyroglobulin.
3. Considerable differences in the composition of neutral and amino sugars were found among amphibian, avian, and mammalian thyroglobulins. Xenopus laevis thyroglobulin was richest in carbohydrate content, whereas chicken thyroglobulin, having a moderate sugar content, revealed a somewhat different neutral sugar composition from that of other thyroglobulins. Even among mammalian thyroglobulins, distinct species specificity was found in most cases. Whale thyroglobulin, in particular, had the lowest neutral and amino sugar content of the thyroglobulins studied. No significant difference was observed between the carbohydrate compositions of human and monkey thyroglobulins.View full abstractDownload PDF (564K) -
I. Reversible Inactivation by Oxidized GlutathioneKunio NAKASHIMA, Kuniko OGINO1973 Volume 74 Issue 3 Pages 601-613
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSFructose 1, 6-diphosphatase [EC 3. 1. 3. 11] from rabbit liver was inactivated by incubation with oxidized glutathione. Other disulfide compounds tested, or reduced glutathione, were without effects. The inactivation reaction proceeded in the neutral pH range, and two apparent pK values were obtained at 4.6 and 7.6. The inactivation was completely prevented by metal cofactors of the enzyme, Mg2+ and Mn2+, although restoration by them of the activity of oxidized glutathione-inactivated enzyme was relatively slow. The inactivation was also prevented and completely reversed by pyridoxal 5'-phosphate, nucleotide tri- and diphosphates or other chelating compounds such as citrate, malonate, EDTA, or 8-hydroxyquinoline. Sulfhydryl compounds such as dithiothreitol or reduced glutathione had no protective or reversal effects on the inactivation reaction, and no decrease of enzyme sulfhydryl groups was detected after inactivation by oxidized glutathione. These results suggested that the inactivation of fructose 1, 6-diphosphatase by oxidized glutatione may be related to the divalent cation binding site, not to the sulfhydryl groups of the enzyme.View full abstractDownload PDF (943K) -
Yew Huat LEE, Khaik Cheang OO1973 Volume 74 Issue 3 Pages 615-621
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSBacillus stearothermophilus B65 showed two stages of active logarithmic growth on a glucose based medium. Its incorporation of 32PO4 into phospholipids was higher at 55°C than at 37°C. At 37°C phosphatidylglycerol was the major phospholipid but at 55°C it was replaced by cardiolipin. Pulse-chase studies showed that turnover of phosphatidylglycerol and cardiolipin was extensive at certain stages of growth and indicated that phosphatidylglycerol could be the precursor of cardiolipin. Turnover rates at 37°C and at 55°C were similar. The proportion of phosphatidylethanolamine was highest when the pH of the medium was low. This phospholipid was stable at 37°C but at 55°C it might undergo a slow turnover.View full abstractDownload PDF (512K) -
Effects of Cortisol, Actinomycin D, and CycloheximideMasao IZAWA, Shogo ICHII1973 Volume 74 Issue 3 Pages 623-626
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
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V. Effects of Metal Ion upon Acidic and Neutral α-Glucosidases, β-Galactosidases, and α-Mannosidases in Liver Extract of RabbitIzumi SUZUKI, Hideo KUSHIDA1973 Volume 74 Issue 3 Pages 627-629
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (171K) -
Ken-ichi KASAI, Shin-ichi ISHII1973 Volume 74 Issue 3 Pages 631-633
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (202K) -
Makoto SASAKI, Taiji KATO, Shigeki IIDA1973 Volume 74 Issue 3 Pages 635-637
Published: September 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (930K)
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