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Reiko SHIMOMURA, Sueo MATSUMURA, Yasutomi NISHIZUKA
1974 Volume 75 Issue 1 Pages
1-10
Published: January 25, 1974
Released on J-STAGE: November 18, 2008
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In human erythrocytes large portions of both adenosine 3', 5'-monophosphate (cyclic AMP
**)-dependent protein kinase [EC 2. 7. 1. 37] and its substrate proteins are associated with membranes. On fractionation of the membrane multiple species of substrate proteins have been distinguished: one is tightly bound to the membrane structure and others are extractable with salt solutions of higher ionic strength. The membrane-bound substrate is heat-stable. After lipid extraction this protein forms highly insoluble polymeric aggregates, but is fully active as substrate for the protein kinase. Before lipid extraction, however, the membrane-bound substrate may be solubilized with lithium diiodosalicylate, but a minimum molecular weight of about 65, 000 has been obtained in the presence of sodium dodecyl sulfate. The soluble substrate proteins extracted from the membrane show relatively small molecular weights ranging from 12, 000 up to about 30, 000. The protein kinase associated with membranes is almost completely extracted as a soluble form with salt solutions. This kinase shows essentially similar kinetic and catalytic properties to many cyclic AMP-dependent protein kinases distributed in soluble fraction of various mammalian tissues.
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Teruo ABE, Kenji TAKAHASHI, Toshio ANDO
1974 Volume 75 Issue 1 Pages
11-22
Published: January 25, 1974
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Porcine brain S-100 proteins were purified by ammonium sulfate fractionation and column chromatography on DEAE-cellulose and Sephadex G-75, and two major S-100 fractions, Fractions 3-2-3 and 4-2-3, were obtained. The amino acid compositions of these fractions were quite different from each other. Upon polyacrylamide gel electrophoresis, Fraction 4-2-3 was found to be homogeneous in both 7.5% and 14% gels. On the other hand, Fraction 3-2-3 was homogeneous in 7.5% gel, but showed heterogeneity in 14% gel. This heterogeneity did not disappear after treatment with β-mercaptoethanol. The presence of calcium ions affects the electrophoretic behavior of Fraction 3-2-3, but not that of Fraction 4-2-3. Both fractions, however, possessed a molecular weight of 26, 000 as determined by gel filtration on Sephadex G-100. When gel electrophoresis was performed in 0.1% sodium dodecyl sulfate in 12.5% gel, Fraction 4-2-3 gave a single band of MW about 19, 000, whereas Fraction 3-2-3 gave two bands of MW about 19, 000 and 7, 000. These results indicate that porcine brain contains several S-100 protein components and that at least some of them are composed of subunits. The results of peptide mapping and N-terminal analysis of Fraction 3-2-3 suggest that this fraction may be a mixture of similar S-100 proteins.
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Tomotaka SHINODA, Yasuharu TSUZUKIDA
1974 Volume 75 Issue 1 Pages
23-44
Published: January 25, 1974
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The reactivity of amino groups of human type K Bence-Jones proteins was investigated by means of trinitrophenylation with sodium 2, 4, 6-trinitrobenzene-1-sulfonate. Lysine-169 of the constant region of the Bence-Jones protein (Ni) appears to be located on the surface of the protein since it is the lysine residue most reactive to TNBS under mild conditions. Lysine-169 of another type K Bence-Jones protein (Ka) was also demonstrated to be highly reactive to the reagent, and therefore the surface position of this lysine seems to be common to all type K Bence-Jones proteins. Lysine-103 of the switch region is less reactive to the reagent and thus appears to be less exposed. Lysine-41/42 of the variable region and lysine-183 of the constant region are much less reactive than any of the above lysine residues. The NH
2-terminal aspartic acid appears to be the least exposed, since it is the least reactive of the rapidly reacting amino groups of type K Bence-Jones proteins. The relative reactivity of these amino groups in the specimen Ni was found to be in the following order: lysine-169〉 lysine-103〉 lysine-41/42〉 lysine-183〉 aspartic acid-1. This order was also found in the specimen Ka.
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II. Spectra of Cytochromes in Respiratory Systems between Liquid Helium and Room Temperatures
Bunji HAGIHARA, Reiko OSHINO, Tetsutaro IIZUKA
1974 Volume 75 Issue 1 Pages
45-51
Published: January 25, 1974
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Absorption spectra of various cytochrome preparations were measured in the visible region over a wide range of temperatures from that of liquid helium (4.2°K) to room temperature (300°K), employing the double Dewar's vessel system of Hagihara and lizuka. The preparations used were purified beef-heart cytochromes
a (
a3), b, and
c1, crystalline pigeon breast-muscle cytochrome
c and crystalline yeast (
Candida krusei) cytochrome
c, all in the reduced form, and crystalline pigeon breast-muscle cytochrome
c in the oxidized form. Remarkable sharpening of each peak in the spectra of the reduced cytochromes, especially of the α-peak, was observed when the temperature of the samples was lowered. In the case of animal cytochromes
c and
c1, the α-peak separated into two distinct peaks (α
1 and α
2) at low temperatures as a result of this sharpening. A wavelength shift of the α-peak occurred toward the blue end (by 3-5nm) when the temperature was lowered from 300°K to about 10°K, except in the case of cytochromes
c and
c1 whose α-peaks were not or were only slightly shifted by peak splitting. Remarkable intensification of extinction was also observed with lowering of the temperature, and this, together with the above sharpening, can be very useful for identification of each cytochrome in mixtures. Com paring the spectra of cytochromes
c1 and
b, whose structures are not known, with those of the well-studied cytochromes
c and
b5, the electronic state and hemeenvironment of cytochromes
c1 and
b are discussed.
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Hidesato OHTSUKA
1974 Volume 75 Issue 1 Pages
53-58
Published: January 25, 1974
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To simplify the composition of the perfusion medium for experiments on the hormonal regulation of hepatic enzymes, the author has developed a new perfusion medium containing Eagle's MEM supplemented by a fluorocarbon suspension as an oxygen donor. The addition of hydrocortisone or dexamethasone induced synthesis of tyrosine transaminase [L-tyrosine: 2-oxoglutarate aminotransferase, EC 2. 6. 1. 5]. However, the addition of insulin, glucagon, or dibutyryl cyclic AMP did not cause enzyme induction. Supplementing the synthetic perfusion medium with serum or with a minute amount of dexamethasone had no discernible effect on enzyme synthesis. Since the infusion of insulin, glucagon, or dibutyryl cyclic AMP induced an increase in the enzyme activity when isolated liver was perfused with blood, other necessary factors for the enzyme induction must be contained in the blood.
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VII. Further Studies on Ca2+-induced Competence
Akira TAKETO, Sigeru KUNO
1974 Volume 75 Issue 1 Pages
59-67
Published: January 25, 1974
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The calcium-dependent transfection system has been further characterized. In chilled CaCl
2 solution, infection of φA replicative-form DNA (RF) is completed within l0min, while at 37°C uptake of the DNA does not occur even after 20-min incubation. The effects of various reagents on the Ca
2+-dependent transfection were investigated. At 50m
M concentration, salts such as KC1 or NaCl caused 30-60% inhibition. The efficiency of transfection is somewhat increased by the addition of 5m
M Mg
2+ and severely reduced by small amounts of Zn
2+. EDTA, at levels above 1m
M, manifests inhibitory action, while 5m
M sodium citrate caused only slight inhibition. The inhibitory effect of EDTA is released by simultaneous addition of Zn
2+. Certain phospholipids such as phosphatidylcholine or phosphatidylethanolamine suppress Ca
2+-dependent infection. Pretreatment of DNA in chilled CaCl
2 with a cell-envelope preparation results in a considerable decrease in the transfectivity, and the DNA-masking activity is sensitive to pronase or organic solvents. Using
14C-labeled RF,
* the effects of various factors on the Ca
2+-dependent binding of DNA were examined. In addition, the competence of several
E. coli mutants was surveyed in relation to their capacity for φA growth.
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Isamu SHIMIZU, Jun NAGAI, Hirohiko KATSUKI
1974 Volume 75 Issue 1 Pages
69-76
Published: January 25, 1974
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The formation and metabolism of acetoacetate in cell-free extracts of aerobically grown
Saccharomyces cerevisiae were studied. The activities of succinyl-CoA: 3-oxoacid CoA-transferase [EC 2. 8. 3. 5] and acetoacetate decarboxylase [EC 4. 1. 1. 4] were detected, but 3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase [EC 4. 1. 3. 4] and 3-hydroxybutyrate dehydrogenase [EC 1. 1. 1. 30] were not found. The CoA transferase seemed to tmdergo a glucose repression. A possible pathway leading to acetone from acetoacetyl-CoA by way of acetoacetate was proposed in yeast. The physiological role of the two enzymes involved are discussed.
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Shizuo HANDA, Kunio YAMATO, Ineo ISHIZUKA, Akemi SUZUKI, Tamio YAMAKAW ...
1974 Volume 75 Issue 1 Pages
77-83
Published: January 25, 1974
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1. After a single injection of H
235SO
4 intraperitoneally into a 6-week-old mouse, the radioactivity of testis seminolipid increased in the first day and decreased to half of the maximum level in one week. The highest incorporation rate was obtained around 10 days after birth.
2. Particulate fraction of boar testis was solubilized with Triton X-100. This enzyme preparation catalyzed the transfer of the sulfate group from PAPS
** to desulfoseminolipid, yielding seminolipid. The reaction was stimulated by the addition of detergents and EDTA, and was inhibited by Mg
2+ and ATP. The enzyme demonstrateda linear response for 30min in the presence of desulfoseminolipid, and had an apparent
Km of 1.7×lO
-3M.
Desulfoseminolipid, galactosylceramide with hydroxy and non-hydroxy fatty acids and lactosylceramide were active as acceptors of sulfate from PAPS. Digalactosylceramide, trihexosylceramide, seminolipid, glucosylceramide, and cholesterol werenot sulfated.
Competition studies suggested that these glycolipids were sulfated by a single enzyme.
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III. Gibberella β-1, 6-Glucan 6-Glucanohydrolase Operative in the Selective Hydrolysis of β-1, 3-Glucosidic Linkages in Eisenia Laminaran
Yuko SHIBATA
1974 Volume 75 Issue 1 Pages
85-92
Published: January 25, 1974
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The hydrolysis of poly- and oligosaccharides of linear structure containing β-1, 3 and β-1, 6-linkages by a purified β-1, 6-glucan 6-glucanohydrolase [EC 3. 2. 1.] from
Gibberella fujikuroi has been studied.
A series of 6-β-lammarioligosyl-glucoses were found together with glucose, laminaribiose, and gentiobiose in the enzymatic hydrolysate of
Eisenia bicyclis laminaran, a linear glucan containing both β-1, 3- and β-1, 6-linkages.
3
2-β-Gentiooligosyl-gentiobioses (O-β-D-Gentiooligosyl-(l-3)-O-β-D-glucopyranosyl-(l-6)-D-glucopyranoses) were isolated from the β-1, 3-glucanase [EC 3. 2. 1. 6] digest of laminaran.
3
2-β-Gentiobiosyl-gentiobiose (Glc-β(l-6)Glc-β(l-3)Glc-β(l-6)Glc) was hydrolyzed into gentiobiose. 3
2-β-Gentiotriosyl-gentiobiose (Glc-β(l-6)Glc-β(l-6)Glc-β(l-3)Glc-β(l-6)Glc) was broken into gentiobiose, gentiotriose, and 6-β-laminaribiosyl glucose (Glc-β(l-3)Glc-β(l-6)Glc).
The initial concentrations of lutean, gentiotetraose, and 3
2-β-gentiobiosyl gentiobiose which give apparent maximal velocities of hydrolysis with
Gibberella β-1, 6-glucan glucanohydrolase were 1.5×lO
-6M, 2.8×lO
-4M, and 3.4×lO
-3M, respectively.
The substrate specificity of the β-1, 6-glucan 6-glucanohydrolase and the hydrolysis of β-1, 3-glucosidic linkages in
Eisenia bicyclis laminaran and oligosaccharides derived from it are discussed.
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Noriko TATEISHI, Taneaki HIGASHI, Shintaro SHINYA, Akiko NARUSE, Yukiy ...
1974 Volume 75 Issue 1 Pages
93-103
Published: January 25, 1974
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1) On starving rats for one or two days their liver glutathione content decreased to between two-thirds and half the normal level. On feeding these animals, it rapidly returned to normal, followed by a gradual increase of glucose-6-phosphate dehydrogenase [EC 1. 1. 1. 49] (G6PD). Maintenance of the liver glutathione level in rats depended upon their food intake.
2) Actinomycin D inhibited the induction of G6PD but did not affect the increase in glutathione concentration. Cycloheximide also failed to inhibit the recovery of the glutathione level. Thus, the rapid increase in the hepatic glutathione level on feeding starved animals did not require
de novo formation of glutathione-synthesizing enzymes.
3) The activities of enzymes involved in glutathione synthesis (γ-glutamylcysteine synthetase [EC 6. 3. 2. 2]+glutathione synthetase [EC 6. 3. 2. 3]) in the liver were similar in starved rats and rats which had been refed.
4) The hepatic concentrations of cysteine and glutamate were reduced in starved animals and increased rapidly on feeding these animals. This may cause increased glutathione synthesis, and can account quantitatively for the rapid rise of the hepatic glutathione content on refeeding. However, the concentration of adenine nucleotides was not favorable for glutathione synthesis in the early stage of refeeding: relatively higher concentrations of ADP and AMP were present, which could inhibit one or both the reactions leading to glutathione synthesis.
5) Glutathione degradation activity in the liver was lower in refed animals than in fasted ones. The turnover of hepatic glutathione was much faster in fasted rats than in refed ones. The degradation rate of glutathione appears to be involved in regulating the hepatic glutathione level.
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Teruo SAWAI, Keiko TORIYAMA, Keiichiro YANO
1974 Volume 75 Issue 1 Pages
105-112
Published: January 25, 1974
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A novel kind of dextranase which is different from the so-far reported dextranases [α-1, 6-glucan 6-glucanohydrolase, EC 3. 2. 1. 11] was purified 44-fold from the culture supernatant of a soil bacterium (
Achromobacter sp.). This dextranase liberates isomaltose from dextrans in an exo-lytic fashion. During digestion of dextrans the degree of polymerization of the reaction products remained 2. Paper chromatograms of digests of dextran showed that the only product was isomaltose. A high-molecular residual substance (limit dextrandextrin), resistant to this enzyme but susceptible to
Penicillium luteum dextranase (endo-type) was recovered after exhaustive digestion of macromolecular dextran by the enzyme. The dextranase split panose into isomaltose and glucose, and isomaltotriitol into isomaltose and sorbitol.
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Masura HONYA, Hideo MIZUNUMA
1974 Volume 75 Issue 1 Pages
113-121
Published: January 25, 1974
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The effect of the presence of various electrostatic and hydrophobic surfactants in the environment on collagen fibrillogenesis has been studied by turbidimetry, and phasecontrast microphotography. The rate of collagen fibril formation was found to be accelerated remarkably in the presence of 10
-4M sodium dodecylbenzenesulfonate or 10
-2-10
-3M non-ionic surfactants with polyoxyethylene groups.
These were found to play different roles in collagen fibril formation. The former anionic surfactant affected the nucleation stage of collagen fibril formation, interacting with the polar regions of the collagen molecule, and brought about subsequent growth of collagen fibrils along nuclei formed longitudinally, as observed by phasecontrast microscopy.
The non-ionic surfactants stimulated all the processes of collagen fibril formation and formed a network structure of thinner collagen fibrils with side branchings, as observed by turbidimetry and phase-contrast microscopy.
These findings indicate the possibility that the mode of initial aggregation in collagen fibrillogenesis under various conditions determines the fiber width, giving rise to different types of fibrous structure of collagen in various tissues.
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Hiroshi SANEMORI, Shusuke YOSHIDA, Takashi KAWASAKI
1974 Volume 75 Issue 1 Pages
123-129
Published: January 25, 1974
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The kinetics of the binding of thiamine pyrophosphate (TPP) to apoenzyme ot partially purified yeast pyruvate decarboxylase [EC 4. 1. 1. 1] have been studied. A quantitative and spectrophotometric determination procedure for the TPP binding step, which is independent of the subsequent coupled alcohol dehydrogenase [EC 1. 1. 1. 1] reaction, has been described.
The binding of TPP to apodecarboxylase occurred rapidly and reached equilibrium after l0min at 25°C when 0.3μ
M TPP was incubated with 100μg of apodecarboxylase in a reaction mixture containing 20m
M Tris-maleate (pH 6.3) and 10m
M MnSO
4. The relative ratio of the rates of TPP binding to apodecarboxylase in the presence of Mn
2+, Mg
2+, and Ca
2+ was 4, 1, and 0.2, respectively. The binding constants for TPP in the oresence of Mn
2+ and Mg
2+ were 0.5μ
M and 25μ
M, respectively, and those for Mn
2+ and Mg
2+ in the presence of 1.2μ
M TPP were 0.29m
M and 2.0m
M, respectively. These results indicalte that the affinity of TPP binding to apodecarboxylase in markedly higher with Mn
2+ than Mg
2+. The role of metal ions in the binding is discussed.
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Hiromichi OKUDA, Yasushi SAITO, Nobuo MATSUOKA, Setsuro FUJII
1974 Volume 75 Issue 1 Pages
131-137
Published: January 25, 1974
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Lipolysis in isolated fat cells was increased by dibutyryl-cyclic AMP (DBcAMP) and adrenaline but not by cyclic AMP.
3H-DBcAMP and
3H-cyclic AMP were incorporated into fat cells to the same extent. Therefore, lack of lipolytic action (free fatty acid release) of cyclic AMP was not due to an inability to be incorporated into the cells.
Adipose tissue was found to contain enough lipase [EC 3. 1. 1. 3] (ediol hydrolyzing activity) to elicit lipolysis even in the absence of lipolytic agents, such as adrenaline and DBcAMP. The amount of lipase did not increase, even in the presence of these lipolytic substances.
Fat cells were disrupted in a hypotonic medium and lipid micelles were collected by centrifugation. These lipid micelles contained lipase and triglyceride. Incubation of these lipid micelles with adrenaline or DBcAMP resulted in marked lipolysis, but Only negligible lipolysis was observed in the absence of these agents.
Adrenaline and DBcAMP did not stimulate lipolysis in homogenates of lipid micelles.
On the basis of these results, the mechanism of the lipolytic action of adrenaline or DBcAMP was discussed.
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I. Purification and General Characteristics
Haruki OKAMURA, Teruo NISHIDA, Hachiro NAKAGAWA
1974 Volume 75 Issue 1 Pages
139-152
Published: January 25, 1974
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Histidine ammonia-lyase [EC 4. 3. 1. 3] was purified approximately 390 fold from female rat liver. The enzyme preparation was shown to be homogeneous and its
s20, W Value was 11.6 by ultracentrifugal analysis. The molecular weight was determined to be 190, 000 by the sedimentation equilibrium method.
On disc-electrophoresis, purified enzyme separated into one major and two minor components having enzyme activity, but after pretreatment with reduced glutathione, the preparation showed only one band. This suggests that the enzyme preparation was pure and that a thiol group is involved in the conversion of polymeric forms to the monomeric from. The isoelectric point was determined to be pH 5.2 by pH gradient electrophoresis.
On immunoelectrophoresis, the purified enzyme gave a single band against antihistidine ammonia-lyase serum.
The enzyme activity was highest between pH 8.8 and 9.0. The
Km value for histidine was calculated to be 1.2×10
-3M.
Thiol compounds, such as glutathione and mercaptoethanol, considerably activated the enzyme. Parachloromercuribenzoate completely inhibited histidine ammonialyase activity at a concentration of 10
-5M and this inhibition was partially reversed by addition of the substrate, histidine. The results indicate that a thiol is involved, not only in the conversion of the associated forms to the dissociated form, but also in the increase in catalytic activity of the enzyme.
EDTA markedly inhibited enzyme activity and this inhibition was reversed effectively by Mn
2+, Zn
2+, and Cd
2+ and less effectively by Ca
2+ and Ni
2+. The activating effect of glutathione was lost in the presence of EDTA and reversed by addition of Mn
2+. These results suggest that a divalent metal ion is essential for the catalytic activity of histidine ammonia-lyase and that thiol is intimately related with its function.
Sodium borohydride and nitromethane, which are known to inhibit bacterial histidine ammonia-lyase activity by reacting with dehydroalanine in the active center, considerably inhibited the enzyme from rat liver.
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Takashi YAMADA, Yasuo NAKAZAWA, Tyunosin UKITA
1974 Volume 75 Issue 1 Pages
153-164
Published: January 25, 1974
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The primary structure of the main component of whale pancreatic ribonuclease (RNase W
1) was studied. The N-terminal amino acid was not found by conventional techniques and was assumed to be N
α-blocked lysine. The C-terminal amino acid was identified as valine. The peptides obtained by cleavage with cyanogen bromide, trypsin, and chymotrypsin were separated by Sephadex G-25 or Dowex 50 X-2 column chromatography and purified by means of paper chromatography or paper electrophoresis. The amino acid sequences of some of the peptides were determined by the Edman-dansyl procedure. It was found that RNase W
1 includes sequences closely similar to those around the active site of ribonuclease A [EC 2. 7. 7. 16] (His-12, Lys-41, and His-119) and their correlation with the enzymatic activity was discussed.
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III. Relationship of Labelled Concanavalin A Binding to the Agglutinability
Hiromi B. MARUYAMA
1974 Volume 75 Issue 1 Pages
165-170
Published: January 25, 1974
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63Ni- and
3H-acetyl labelled concanavalin A's (con A) were tound to agglutinate protease-treated spheroplasts of
E. coli by about one-third and slightly less than the original con A, respectively. However, both radioactively labelled con A derivatives apparently bound to the spheroplasts in the same manner. The total amount of labelled con A's bound per spheroplast was slightly less with protease-treated spheroplasts than non-treated ones, which were not agglutinated by con A. The number of con A molecules bound per spheroplast was in the range of 6-8×10
5, approximately one-hundredth of the molecules bound to a transformed mammalian cell, as reported elsewhere. Methyl α-D-glucoside (αMG) showed at most 50% inhibition of con Abinding at a concentration sufficient to inhibit agglutination completely
Specific binding of con A molecules to αMG sites was found to be higher with protease-treated spheroplasts (2.7-3.8×10
5) than with non-treated ones (2.2-2.4×10
5). When incubation was performed at temperatures lower than 37°C, than agglutination was reduced greatly or completely at 0°C, whereas the binding was inhibited by only 20% at most. From these results the relationship between the binding of con A on the spheroplast surface and the inhibition of agglutination was discussed in relation to observations in the transformed animal cell-con A system.
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Makoto SASAKI, Hisako YAMAMOTO, Hiroyasu YAMAMOTO, Shigeki IIDA
1974 Volume 75 Issue 1 Pages
171-177
Published: January 25, 1974
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The mode of inhibition of proteolytic enzymes of different origins (animal, plant, and bacteria) and of different groups (serine and cysteine enzymes) by human serum proteinase inhibitors was investigated. The inhibitors which interacted with these enzymes were identified by suppressing their inhibitory actions on these proteolytic enzymes, using monospecific antibodies against the individual serum proteins. The inhibitor α
1-antitrypsin predominantly inhibited the serine enzymes of animal origin trypsin [EC 3. 4. 4. 4] and chymotrypsin [EC 3. 4. 4. 5], and had less effect on the serine enzyme of bacterial origin nagarse (subtilisin BPN') [EC 3. 4. 4. 16], and no inhibitory effect on the enzymes of plant origin papain [EC 3. 4. 4. 10], ficin [EC 3. 4. 4. 12], and stem bromelain [EC 3. 4. 4. 24]. In contrast α
2-macroglobulin inhibited all kinds of proteolytic enzymes irrespective of their enzyme groups or origins. From these it is concluded that 1) serum proteinase inhibitors have the potentiality to inhibit foreign proteolytic enzymes, 2) α
1-antitrypsin seems to have a fairly broad specificity for serine enzymes of animal origin and of other origins, and 3) α
2-macroglobulin can combine with both serine and cysteine enzymes, regardless of the stereospecificities of their active sites.
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Tairo OSHIMA, Kazutomo IMAHORI
1974 Volume 75 Issue 1 Pages
179-183
Published: January 25, 1974
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Deoxyribonucleic acid was extracted from an extremely thermophilic bacterium and its physicochemical properties were investigated. The melting temperature in 0.15
M sodium chloride, that in 0.015
M sodium chloride, and the density in cesium chloride were, respectively, 97.5°C, 81.3°C, and 1.727. The guanine plus cytosine content of the DNA was estimated to be 68% from these values, and this is in good accord with the GC content found by acid hydrolysis. The circular dichroic spectrum suggested that the nucleic acid contains base pairs with a different conformation from the ordinary B form. No significant difference was observed between the priming activities of thermophile and mesophile DNA's for mesophile RNA polymerase [EC 2. 7. 7. 6].
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Marie-Thérèse PLANCOT, Kia-Ki HAN
1974 Volume 75 Issue 1 Pages
185-188
Published: January 25, 1974
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Hideaki HIGASHINO, Masao TAKEDA
1974 Volume 75 Issue 1 Pages
189-191
Published: January 25, 1974
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Satoshi OMURA, Hideo TAKESHIMA
1974 Volume 75 Issue 1 Pages
193-195
Published: January 25, 1974
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Tamotsu TAKETOMI, Atsushi HARA, Nariko KAWAMURA, Masayo HAYASHI
1974 Volume 75 Issue 1 Pages
197-199
Published: January 25, 1974
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Kenji TAKAHASHI
1974 Volume 75 Issue 1 Pages
201-204
Published: January 25, 1974
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James B. ENGLE, Oscar G. WARD
1974 Volume 75 Issue 1 Pages
205-209
Published: January 25, 1974
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Setsuro EBASHI, Shun-ichi OHNISHI, Shin-ichi ABE, Koscak MARUYAMA
1974 Volume 75 Issue 1 Pages
211-213
Published: January 25, 1974
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