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Volume 71, Issue 1
Displaying 1-23 of 23 articles from this issue
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Radha PANT, Indira Dyna MORRIS1972 Volume 71 Issue 1 Pages 1-8
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe variation of alkaline and acid phosphatases [EC 3. 1. 3. 1 and 2], glycogen, inorganic phosphorus (Pi), citrate, total free sugars and protein concentration in the fat body of Philosamia ricini were studied. The results obtained indicate that acid phosphatase activity predominates over that of the alkaline phosphatase all through development while the latter (alkaline phosphatase) shows very little activity which is almost negligible in comparison with the former (acid phosphatase). The high acid phosphatase activity which varies during pupal development is suggestive of its importance in pupal development and reproduction. It could also be related to an active glycogen mobilization with dephosphorylation mechanism at the acid range. The rate of glycogen degradation appears to be influenced by similar increase in inorganic phosphorus and phosphorylase [EC 2. 4. 1. 1] activity. This suggests that high concentration of inorganic phosphorus inhibits glycogen synthesis and conversely while maintained at a low level, glycogen synthesis is enhanced. Citrate appears to play an important role in glycogen metabolism by its inhibitory effect of glycolysis which needs further experimental confirmation in this insect. This inhibition facilitates mobilization of increased quantity of glycogen thus providing ATP for protein biosynthesis.View full abstractDownload PDF (764K) -
I. Isolation of GlycoproteinsEiji SHIMADA, Toshijiro YAMAGUCHI, Go MATSUMURA1972 Volume 71 Issue 1 Pages 9-16
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Approximately a half of the hexosamine and all of the uronic acid in a 0.5M NaCl extract of rabbit skin were precipitated by cetylpyridinium chloride (CPC). Ethanol was added to the CPC supernatant until the final concentration of ethanol reached to 70%, and thus the CPC supernatant was separated into two fractions, 70% EtOH supernatant and 70% EtOH precipitate.
2. From 70% EtOH precipitate, four albumin-like glycoprotein fractions were obtained. The carbohydrate contents and compositions of two of the four fractions were quite similar to each other, and the carbohydrate contents of the two were higher than those of the other two fractions, whose sugar contents were again similar to each other except for the contents of fucose and sialic acids. Hexoses (galactose, mannose, and glucose), glucosamine, fucose, and sialic acids were present in all of the four glycoprotein fractions.
3. From 70% EtOH supernatant were isolated two glycoproteins, which contained galactose, mannose, glucosamine, and small amounts of fucose and sialic acids. The content of carbohydrate was about 60% in one glycoprotein and about 50% in the other. The latter contained hydroxyproline.View full abstractDownload PDF (675K) -
I. Demonstration and Characterization of Aal Allotypic Determinants Specific for IgGAkira SETO1972 Volume 71 Issue 1 Pages 17-27
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA difference was observed in the Aal allotypic specificities of IgG and IgM in the precipitation reaction in agar gel, indicating the existence of allotypic determinants specific for IgG. This was confirmed by absorption experiments using anti-allotypic serum. These allotypic determinants were not found on IgM or its fragments, IgMs and Fabμ. They were localized on IgG molecules of one of two variants of Aal specificity and on its Fab fragment; all IgG molecules carrying these determinants seemed to possess allotypic determinants of the variant and conversely all molecules of the variant seemed to carry these determinants. A distribution study of these determinants, in a certain population of rabbits, demonstrated that their existence is closely linked to the existence of Aal allotypic specificity. In rabbits in which phenotypic expression of Aal specificity was suppressed by neonatal treatment with anti-Aal serum, the expression of the allotypic determinants specific for IgG was also suppressed and this suppressed state continued as long as expression of the former specificity remained suppressed. The two variants of Aal allotypic specificity were observed in IgM as well as IgG and seemed to have certain allotypic determinants in common.View full abstractDownload PDF (2998K) -
Tahei NEGI, Tatsuya SAMEJIMA, Masachika IRIE1972 Volume 71 Issue 1 Pages 29-37
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS(1) In order to investigate the role of tryptophan residues on the activity of inorganic pyrophosphatase [EC 3. 6. 1. 1, PPiase], several lines of experiments were carried out.
(2) Methylenediphosphonate (PCP) was found to be a competitive inhibitor for PPiase, and its Ki value was found to be 1.1×10-3M at pH 6.0.
(3) The ORD curve of PPiase-Mg2+PCP complex showed the decrease of the depth of trough at 233mμ and apparent change of the Cotton effect around 290mμ in shape comparing with the ORD curve of PPiase. The CD curve of PPiase-Mg2+PCP complex showed a slight blue shift of negative CD band around 290mμ from that of PPiase.
(4) The difference spectrum between PPiase and PPiase bound with Mg2+PCP had a negative peak at 300mμ indicating the possible participation of tryptophan residues for enzyme-inhibitor complex. These results suggested that the environment around some tryptophan residues was changed by the binding with Mg2+PCP.
(5) About one mole of tryptophan residue of PPiase was oxidized by NBS at pH 6.0-6.5 with simultaneous loss of the enzymatic activity. The rate of NBS oxidation was suppressed by the presence of Mg2+PCP. PPiase which was oxidized with NBS lost its Cotton effect around 290mμ. These experiments described above showed that the tryptophan residue has an important role on the enzymatic activity.
(6) The fluorescence emission spectrum of PPiase excited by 295mμ light was found to have maximum at 330mμ and the maximum was shifted to 350mμ in 6M guanidine-HCl. The pH dependence of fluorescence emission maximum indicated that at pH 6.0-7.5 where most of our experiments were carried out, the amount of tryptophan residues exposed to the solvent was minimum.
(7) Solvent perturbation difference spectra of PPiase in the presence and absence of Mg2+PCP using ethylene glycol as a perturbant, gave two peaks at 285mμ and 278mμ and a shoulder at 295mμ. By comparing Δε at peak positions with those of N-acetyltyrosinamide and N-acetyltryptophan, it was suggested that about 10 residues of tyrosine and 2.5 residues of tryptophan were exposed to the solvent in the absence of Mg2+PCP, and that 5 residues of tyrosine and 1.4 residues of tryptophan were exposed in the presence of Mg2+PCP.View full abstractDownload PDF (727K) -
II. ATPase Activity at Acid pHMasaaki KURODA, Koscak MARUYAMA1972 Volume 71 Issue 1 Pages 39-45
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSEnzymatic properties of F-actin ATPase [EC 3. 6. 1. 3] at acid pH were investigated in details with a special reference to the formation of paracrystals. The pH optimum was around pH 4.7 at 45°C. The apparent activation energy was 22kcal/mole. At pH 5.0 and 45°C, the ATPase activity was proportional to both protein concentration and incubation time, and the specific activity was approximately 0.3μmole/mg/hr. The apparent Michaelis constant was 4×10-4M. Ca and Mg ions inhibited the ATPase activity, while K ion enhanced it up to 0.4M. The substrate specificity was found to be so broad that ITP, UTP, CTP, GTP and deoxyATP were hydrolyzed at a similar rate to ATP. However, ADP, inorganic triphosphate and adenosine tetraphosphate were not dephosphorylated. Based on the rapid exchange reaction of the bound nucleotide with added ATP, it was concluded that ATP splitting was due to “partial interruption” of F-actin structure at acid pH. The ATP splitting action at acid pH may indicate the dynamic state of F-actin which eventually leads to the formation of the paracrystal (Type I), although the ATP splitting is not the only necessary factor.View full abstractDownload PDF (538K) -
Yoshikazu YANAGI, Ichiro SEKUZU, Yutaka ORII, Kazuo OKUNUKI1972 Volume 71 Issue 1 Pages 47-56
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Heme a, the prosthetic group of cytochrome oxidase [EC 1. 9. 3. 1], was extracted from bovine heart muscle and purified by chromatography on a DEAE-cellulose column.
2. The relationship between the absorption spectra and state of aggregation of heme a in solution was investigated. Heme a was found to be polymeric in a phosphate buffer solution, and converted to the dimeric form by non-ionic detergents.
3. The reaction of heme a with imidazole and HCN was studied in the anionic (sodium dodecyl sulfate), non-ionic (Triton X-100), and cationic (cetyltrimethylammonium bromide) solutions. Heme a reacted with imidazole to form a di-imidazole complex, but the reactivities were different depending on the ionic nature of the detergents used; heme a reacted with imidazole more easily in the anionic detergent solution than in the cationic. HCN reacted not only with the heme iron but also with the formyl group of heme a to form cyanhydrin in the neutral pH region, but not on the alkaline side. For induction of a spectral change of the same extent, a higher concentration of HCN was required in the anionic detergent solution than in the cationic.
4. The reaction of the formyl group of heme a with HCN was investigated in detail in a Triton X-100 solution containing imidazole. It was established that the reactivity of the formyl group was dependent on the redox state of the heme iron; it was more reactive in the oxidized form than in the reduced.View full abstractDownload PDF (863K) -
III. Purification and Some Enzymatic Properties of Aspergillus carneus DextranaseNobutsugu HIRAOKA, Juichiro FUKUMOTO, Daisuke TSURU1972 Volume 71 Issue 1 Pages 57-64
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Aspergillus carneus dextranase [α-1, 6-glucan 6-glucanohydrolase, EC 3. 2. 1. 11] was purified about 60-fold by means of ammonium sulfate fractionation, repeated chromatography on a column of DEAE-cellulose and gel filtration on Bio Gel P-150.
2. The enzyme preparation was further fractionated into two fractions, dextranase I (pI4. 12) and dextranase II (pI4. 35) by isoelectric focusing.
3. The purified dextranase I was homogeneous as examined by ultracentrifugal analysis and by disc electrophoresis. Dextranase II was also homogeneous in disc electrophoresis.
4. Both enzymes were most active at pH values between 5.0 and 5.5 in 10-min reaction and stable over a pH range from 4.5 to 9.0 at 30°C for 24 hr. Some heavy metal ions, such as Cu2+, Hg2+, Fe3+ and Ag+, were found to inactivate both the enzymes.
5. Values of 71, 000 for the molecular weight and 4.8S as s20, w were obtained by ultracentrifugal analyses of the dextranase I.View full abstractDownload PDF (1371K) -
Kunio KITAMURA, Ikuo YAMASHINA1972 Volume 71 Issue 1 Pages 65-76
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Reduced and alkylated α1-acid glycoprotein (α1-AGP) was cleaved into three frag-ments by means of cyanogen bromide oxidation of which one was a glycopeptide (CB-I) containing all the carbohydrates of α1-AGP, and other two were carbohydrate-free peptides. CB-I had no free NH2-terminal amino acid, corresponding to the NH2-terminal half of α1-AGP.
2. CB-I was digested with trypsin after the modification of lysine or arginine residues. Glycopeptides isolated from the tryptic digests with a total of about 100 amino acid residues were analyzed for the amino acid sequence using Edman procedures, which gave sequences of 69 amino acid residues. It was remarkable that some of the glycopeptides had partially overlapping sequences, which suggested the presence of regions in which amino acid sequences are variable.
3. A triplet structure, Asn (-CHO)-X-Ser (or Thr), was present in all the determined sequences.View full abstractDownload PDF (1010K) -
Hajime YAMASAKI, Kazumi YAMASAKI1972 Volume 71 Issue 1 Pages 77-83
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSIt was demonstrated that 7α-hydroxycholesterol-14C administered to a hen furnished with a bile-fistula was converted not only to the common primary bile acids but also to 3β, 7α-dihydroxychol-5- and -4-enoic acids, the latter of which has recently been isolated from bladder bile of hens.
As a metabolite of the 7α-hydroxy sterol-14C, allocholic acid was also identified and its natural occurrence in bladder bile once reported was confirmed (see “RESULTS”).View full abstractDownload PDF (1487K) -
Yoshikazu AYAKI, Kazumi YAMASAKI1972 Volume 71 Issue 1 Pages 85-89
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA Lifschütz positive compound was found in the bile of bile-fistula rats injected with mevalonate-14C or with cholesterol-14C. This compound was identified as 3β, 7α-dihydroxychol-5-enoic acid by thin-layer chromatography and radio-isotope dilution experiments. This finding was taken for a further evidence favorable for a new pathway of chenodeoxycholic acid biogenesis proposed by the authors.View full abstractDownload PDF (418K) -
I. The Internal Freedom of Tropomyosin in the Complex of Troponin-tropomyosin-F-actinKoshin MIHASHI1972 Volume 71 Issue 1 Pages 91-97
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA conjugate of rabbit skeletal tropomyosin with fluorescein isothiocyanate (TM*) was combined with F-actin (F) and troponin (TN) (both from rabbit skeletal muscle). Fluorescence polarization of the complexes of F-TM* and F-TM*-TN in the presence or absence of Ca ion were examined as a function of temperature in order to see the internal freedom of motion of tropomyosin in the protein complex.
The degree of fluorescence polarization around room temperature was indistinguishable between F-TM* and F-TM*-TN, giving a single rotational relaxation time of the order of 40 nanoseconds. Above 34°C, a new rotational motion (12 nanoseconds) appeared in F-TM*-TN while F-TM* showed no alteration. The new rotational motion in F-TM*-TN was independent of the Ca-binding state of troponin. The Ca-binding state of troponin affected the internal freedom of tropomyosin above 43°C; if troponin was binding Ca ion the freedom of tropomyosin increased and if troponin was devoid of Ca ion tropomyosin was strongly captured to F-actin. This splitting of the internal freedom of tropomyosin was likely related to an alteration of F-tropomyosin (TM) interaction above 43°C.View full abstractDownload PDF (633K) -
Makoto KITO, Shigeo AIBARA, Kiyozo HASEGAWA, Tadao HATA1972 Volume 71 Issue 1 Pages 99-105
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSAcyl-CoA: L-glycerol 3-phosphate acyltransferase [EC 2. 3. 1. 15] from E. coli is a particulate enzyme, which was found to be inhibited by cis-9, l0-methylenehexadecanoate. The inhibition was noncompetitive with respect to L-glycerol 3-phosphate. Palmitate, elaidate, and trans-vaccenate showed no inhibition of the acyltransferase, whereas palmitoleate, oleate, and cis-vaccenate inhibited. cis-9, l0-Methylenehexadecanoate was approximately twice as inhibitory as mono-olefinic acids. The free fatty acids in the cells were also found to vary with different growth phases. There was a ten-fold increase in the amount of free cis-9, l0-methylenehexadecanoic acid in the cells from the early exponential to the stationary phase.View full abstractDownload PDF (509K) -
II. Substrate Specificity of the EnzymeTomohiro MEGA, Tokuji IKENAKA, Yoshio MATSUSHIMA1972 Volume 71 Issue 1 Pages 107-114
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSN-Acetyl-β-D-glucosaminidase [EC 3. 2. 1. 30] isolated from Takadiastase (Sankyo) hydrolyzed partially O-methylated N-acetyl-chitooligosaccharides to produce N-acetyl-glucosamine, 3-O-methyl-, 6-O-methyl- and 3, 6-di-O-methyl-N-acetylglucosamines. Phenyl 3-O-methyl- and 6-O-methyl-N-acetyl-β-D-glucosaminides were also hydrolyzed by the enzyme, whereas phenyl 3, 4-di-O-methyl-N-acetyl-β-D-glucosaminide was not hydrolyzed.
N-Acetyl-β-D-glucosaminidase activity was inhibited by acetamido-compounds such as acetamide, acetanilide, and N-acetylglucosamine. N-Propionylglucosamine and N-formylglucosamine showed inhibitory action weaker than N-acetylglucosamine.
These results indicated that the hydroxyl at carbon 4 and acetamido at carbon 2 of the substrate were significant in the formation of ES-complex.
Fairly high specificity for the aglycon part of the substrates was recognized in a study of the hydrolysis rates of 1-L-β-aspartamido-2-acetamido-1, 2-dideoxy-β-D-glucose, N-acetylglucosaminyl-β(1-4)-N-aeetylmuramic acid, N-acetylglucosaminyl-β(1-4)-N-acetylglucosaminitol and di-N-acetylchitobiose.View full abstractDownload PDF (1349K) -
XI. Formation and Decomposition of the Reactive Myosin-Phosphate-ADP ComplexAkio INOUE, Kazuko SHIBATA-SEKIYA, Yuji TONOMURA1972 Volume 71 Issue 1 Pages 115-124
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe amount and rate of formation of the reactive myosin-phosphate-ADP complex, EADPP, was estimated by measuring the size and rate of the initial burst of Pi-liberation after stopping the reaction by trichloroacetic acid. Measurements on myosin-ATPase [EC 3. 6. 1. 3] were made in 0.5M KCl and 2.5mM MgCl2 at pH 7.8 and 0°C, unless otherwise stated. The following results were obtained. 1) At ATP concentrations below 0.3μM, the values of KM and Vfm for formation of EADPP were O.3μM and 0.70 mole Pi/min•4.8×105g myosin, respectively, while at ATP concentrations above 0.3μM, the values of KM, and Vfm were much larger. 2) The values of KM and Vfm of actomyosin-ATPase were measured in 50mM KCl and 2mM MgCl2 at pH 7.0 and 25°C. At ATP concentrations below 10μM, they were 2.9μM and 2.5×102moles/min•4.8×105g myosin, respectively, and were equal to those for EADPP formation of myosin under the same conditions. At ATP concentrations above 10μM, the rate of the actomyosin-ATPase reaction was larger than that expected from the KM and Vm values obtained at low ATP concentrations. 3) At ATP concentrations above 0.5μM, the values of KM and Vm, of myosin-ATPase in the steady state were 1μM and 0.44 mole Pi/min•4.8×105g myosin, respectively, while at ATP concentrations below 0.3μM, the rate of the ATPase reaction was almost independent of the ATP concentration and had a Vm value of about 1/4 of that obtained at high ATP concentrations. 4) The results of Lymn and Taylor on the dependence of the burst size on the ATP concentration was reexamined in 0.5M KCl and 10mM MgCl2 at pH 8.0 and 20°C. Both the rate in the steady state and the size of the initial burst of Pi-liberation were found to be independent of the ATP concentration at concentrations of 5 to 200μM.View full abstractDownload PDF (827K) -
Effect of Thyroxine on Phosphoenolpyruvate Carboxykinase in Rat Liver in Normal and Cold EnvironmentsKatsuya NAGAI, Hachiro NAKAGAWA1972 Volume 71 Issue 1 Pages 125-131
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSTaking the diurnal variation of enzyme activity into account, the action of thyroid hormone on rat liver phosphoenolpyruvate carboxykinase [EC 4. 1. 1. 32] was investigated. The results obtained were as follows; 1) Thyroidectomy diminished the enzyme activity and L-thyroxine significantly enhanced it either in intact rats or in thyroidectomized rats. The dose of L-thyroxine required for significant increase in the enzyme activity 24 hr after a single injection was as little as 10μg per 100g body weight, and significant activation was observed 6 hr after injection of 50μg per 100g body weight into thyroidectomized rats. 2) The activation of the enzyme by thyroxine was almost completely blocked by cycloheximide. 3) The adrenal gland was not essential for the increase in enzyme activity caused by thyroxine. 4) Thyroid hormone was not the sole essential factor for induction of the enzyme after cold-exposure.View full abstractDownload PDF (576K) -
I. Amino Acid Compositions and Sequences of Tryptic PeptidesKoki YOKOTSUKA, Aiko KIKUCHI, Kensuke SHIMURA1972 Volume 71 Issue 1 Pages 133-146
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The alanine-rich, arginine-rich histone from calf thymus, the homogeneity of which was evidenced by gel electrophoresis, N-terminal amino acid analysis and amino acid analysis, was fractionated and purified by fractional extraction, countercurrent distribution and gel filtration.
2. This histone has been estimated to contain 135 to 140 amino acid residues (a molecular weight of approximately 14, 000) based on amino acid analysis and N-terminal (alanine) and C-terminal (alanine) amino acid analyses, distributing as follows: Lys12, Lys(Me)1-2, His2, Arg18, Cys1-2, Asp6, Thr11, Ser4-5, Glu16, Pro6-7, Gly7, Ala19, Va16, Met2, Ile6-7, Leu12, Tyr2 and Phe4.
3. Sequence studies on the alanine-rich, arginine-rich histone have been started by tryptic hydrolysis and isolation of the resulting peptides by ion-exchange chromatog-raphy, gel filtration and paper chromatography. Twenty soluble peptides and an insoluble core peptide were isolated, and the analysis of the amino acid compositions of the peptides and the determination of the sequences of 16 of these peptides were Derformed.View full abstractDownload PDF (1541K) -
Munekazu SHIGEKAWA, Yuji TONOMURA1972 Volume 71 Issue 1 Pages 147-149
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
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Hiromichi OKUDA, Setsuro FUJII1972 Volume 71 Issue 1 Pages 151-152
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
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Tamio HIRABAYASHI, Yujiro HAYASHI1972 Volume 71 Issue 1 Pages 153-156
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
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Hirobumi TERAOKA, Shigetaka NAITO, Katsura IZUI, Hirohiko KATSUKI1972 Volume 71 Issue 1 Pages 157-160
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
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Kenji TAKAHASHI, Fumio MIZOBE, Wen-Jong CHANG1972 Volume 71 Issue 1 Pages 161-164
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
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Takehiko KOIDE, Susumu TSUNASAWA, Tokuji IKENAKA1972 Volume 71 Issue 1 Pages 165-167
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
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Shin-ichi ABE, Koscak MARUYAMA1972 Volume 71 Issue 1 Pages 169-171
Published: January 25, 1972
Released on J-STAGE: November 18, 2008
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