巻号一覧
69 巻, 5 号
選択された号の論文の19件中1～19を表示しています
- |<
- <
- 1
- >
- >|
-
Machiko ICHIMURA, Kinji KSUKADA1971 年 69 巻 5 号 p. 823-828
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリーA polynucleotide kinase, which catalyzes the phosphorylation of 5'-hydroxyl ends of deoxyribonucleic acid in the presence of adenosine triphosphate, was extracted from rat liver nuclei. Its optimal pH was 5.5. It was thermolabile and completely dependent on the presence of Mg2+ for activity. p-Chloromercuribenzoate inactivated this enzyme and this inactivation was overcome by mercaptoethanol. The 32P labeled DNA products of this reaction resulted in the release of 32P by the action of alkaline phosphatase [EC 3. 1. 3. 1] or deoxyribonuclease [EC 3. 1. 4. 5]. There is no striking difference in specific activity of this enzyme between normal and partially hepatectomized rat livers.抄録全体を表示PDF形式でダウンロード (332K) -
III. The Regulation of Liver Serine Dehydratase and Ornithine δ-Aminotransferase in Hypophysectonmized-pancreatectomized R_??_Katsuyuki NAKAJIMA, Eiji ISHIKAWA1971 年 69 巻 5 号 p. 829-837
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリーRoles of pituitary, adrenocortical and pancreatic hormones in the regulation of liver serine dehydratase [EC 4. 2. 1. 13] and ornithine δ-aminotransferase [EC 2. 6. 1. 13] were studied by using hypophysectomized-pancreatectomized rats. The activities of liver serine dehydratase and ornithine δ-aminotransferase in hypophysectomized-pancreatectomized rats (3 days after the removal of pancreas) were reduced to one tenth and one fourth, respectively, of those in hypophysectomized rats, and liver histidase activity was also significantly decreased. This indicates that pituitary hormones including growth hormone play no significant role to depress those enzyme activities in pancreatectomized rats and supports the concept that those enzyme activities in rat liver are maintained by pancreatic hormone(s) other than insulin. Twenty-four hour-treatment with hydrocortisone acetate had no effect on liver serine dehydratase activity in hypophysectomized-pancreatectomized rats but markedly potentiated the enzyme induction by glucagon and dibutyryl cyclic AMP. The level of liver ornithine δ-aminotransferase was elevated slighly by glucagon, but not significantly by dibutyryl cyclic AMP, and much elevated consistently by the simul-taneous administration of hydrocortisone acetate and glucagon or dibutyryl cyclic AMP in hypophysectomized-pancreatectomized rats. It is not conclusive whether the effects of hydrocortisone acetate and glucagon or dibutyryl cyclic AMP on liver ornithine δ-aminotransferase are synergistic or additive, since the enzyme activity was not increased consistently on administration of hydrocortisone acetate alone. Sixty-four hour-treatment with hydrocortisone acetate of hypophysectomized-pancrea-tectomized rats did not result in a consistent enhancement of the two enzyme activities, but it was shown by using younger pancreatectomized rats weighing 120 to 130g that both enzyme activities could be raised by 48hour-treatment with hydro-cortisone acetate even in the absence of pancreatic hormones. No effect on both enzyme activities in hypophysectomized-pancreatectomized rats were observed by force-feeding amino acid mixture 4 times during 24hr.抄録全体を表示PDF形式でダウンロード (623K) -
Tetsuro YOSHIMURA, Toshizo ISEMURA1971 年 69 巻 5 号 p. 839-846
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリーGlucose oxidase [β-D-glucose: O2 oxidoreductase, EC 1. 1. 3. 4] was purified by using DEAE-cellulose. The purified enzyme was homogeneous with respect to ultracentrifugal and electrophoretical criteria.
The subunit structure of the glucose oxidase was investigated by the sedimentation velocity and sedimentation equilibrium analyses. The sedimentation coefficient and the molecular weight of the native enzyme were calculated to be 7.5S and 160, 000, respectively. In 6M guanidine hydrochloride (pH 3.0), they were reduced to 3.3S and 81, 000, respectively. A sedimentation coefficient of 2.8S and a molecular weight of 45, 000 were obtained for the enzyme in 6M guanidine hydrochloride (pH 8.0) containing 0.3M mercaptoethanol. In 6M guanidine hydrochloride (pH 3.0), the sulfhydryl content of the glucose oxidase was estimated to be 1.8 moles per mole enzyme. The sulfhydryl content increased to 5.9 moles by treatment with 0.3M mercaptoethanol in 6M guanidine hydrochloride (pH 8.0), which indicated that the glucose oxidase had two sulfhydryl and two disulfide groups.
From these results, it is concluded (1) that the glucose oxidase molecule consists of four polypeptide chains equal in molecular size, and (2) that two polypeptide chains are held together by a disulfide bond to form a dimer, and two dimeric units associate noncovalently to form a tetramer.抄録全体を表示PDF形式でダウンロード (1879K) -
Hidekazu IWASAKI, Teruo MATSUBARA1971 年 69 巻 5 号 p. 847-857
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリー1. Cytochrome c-557 (551) was prepared from Alcaligenes faecalis. The molecular weight was 65, 000. The haem groups were not split off by the ordinary acid-acetone treatment and, in the presence of pyridine, a normal c-type haemochrome was formed. The cytochrome was found to be a dihaem protein. The reduced form of this cytochrome reacted with CO and the oxidized one with cyanide at pH 7.
2. A two-haem cytochrome (cytochrome cd) was crystallized from the same organism. The molecular weight was 90, 000. This cytochrome contained a c-type haem and a d-like haem, and two atoms of iron per molecule. The c-haem seems to be responsible for its typical α peak with a shoulder. The d-like haem reacted with CO, CN-, NO2- and NO under different conditions. Cytochrome cd had a strong nitrite reductase activity.
3. This microorganism had a strong denitrifying activity in anaerobic condition. The cytochrome c-557 (551) was present in the cells grown in the absence of nitrate and nitrite, whereas the cytochrome ed and a small quantity of cytochrome c-557 (551) were present in the cells grown in the presence of nitrate or nitrite. Both cytochromes were absent in the cells grown under high aeration.抄録全体を表示PDF形式でダウンロード (2562K) -
Teruo MATSUBARA, Hidekazu IWASAKI1971 年 69 巻 5 号 p. 859-868
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリー(1) Reduction of nitrite, nitric oxide and nitrous oxide by Alcaligenes faecalis grown anaerobically in a nitrate-containing medium was examined.
(2) When lactate was used as electron donor, the resting cells produced nitrogen from nitrite. Azide (10-2M) decreased the rate of gas formation and the gas formed was identified as nitrous oxide. Cyanide (10-4M) also inhibited gas formation, and the gas formed was identified as nitric oxide and nitrous oxide. Conversion of nitrous oxide to nitrogen was inhibited completely in the presence of KCN or NaN3. The reduction of nitric oxide to nitrous oxide was strongly inhibited by KCN. Hydroxylamine was not utilized as a source of nitrogenous gas product, but was a strong inhibitor for nitrite reduction.
(3) Cell-free extracts could produce only nitrous oxide from nitrite or nitric oxide. Phenazine methosulfate with ascorbate was found to be a good electron donor for nitrite and nitric oxide reduction.
(4) Cytochrome cd was suggested to function as nitrite reductase which converted nitrite to nitric oxide.
(5) Nitric oxide reductase, which catalyzed the reduction of nitric oxide to nitrous oxide and existed mostly in the particulate fraction, was partially obtained in the soluble fraction. It was suggested that an inhibitory substance capable of masking nitric oxide reductase activity was present in the soluble fraction.抄録全体を表示PDF形式でダウンロード (560K) -
III. Further Purification of Components I and II and Their Functions in Tyrocidine SynthesisKazuo FUJIKAWA, Yohko SAKAMOTO, Kiyoshi KURAHASHI1971 年 69 巻 5 号 p. 869-879
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリー1. Two complementary fractions of tyrocidine-synthesizing system, Components I and II, were purified from a crude extract of Bacillus brevis ATCC 8185 by means of ammonium sulfate fractionation, protamine sulfate precipitation, DEAE-cellulose and hydroxylapatite column chromatography. Molecular weights of 100, 000 and 290, 000, were obtained for Components I and II, respectively, by sucrose density gradient centrifugation.
2. D- and L-phenylalanine activating activity was found in Component I. Component II possessed the activating activities of all the constituent amino acids of tyrocidine. ATP-dependent phenylalanine racemase activity was detected in Component I. Component I bound D-phenylalanine and Component II bound all constituent amino acids tested. The binding required ATP, Mg2+ ion and probably free sulfhydryl groups in the enzyme.
3. In the synthesis of tyrocidine, Component I could be replaced by the phenylalanine racemase preparation purified from Bacillus brevis Nagano, a gramicidin Sproducing bacterium.
4. The results obtained clarify the function of the two components, i.e., Component I is concerned with the formation of the D-phenylalanine residue and Component II with the activation of the other amino acids and peptide formation. Tyrocidine synthesis possibly takes place through intermediates of aminoacyl-adenylate and aminoacyl-enzyme complexes.抄録全体を表示PDF形式でダウンロード (1294K) -
Masachika IRIE, Masatomi HARADA, Tahei NEGI, Tatsuya SAMEJIMA1971 年 69 巻 5 号 p. 881-892
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリー1) The process for purification of ribonuclease [EC 2. 7. 7. 17] (RNase M) from Aspergillus saitoi was improved. The yield was about twice that reported previously. The purified enzyme was homogeneous by gel electrophoresis.
2) The molecular weight of RNase M was estimated to be 38, 000 by gel filtration on Sephadex G-75.
3) The amino-, and carboxyl-terminal amino acids of RNase M were determined to be threonine and serine, respectively.
4) The amino acid composition of RNase M was determined.
5) RNase M contained about 7.21.7 neutral sugar (mannose and glucose) and 1.65%glucosamine.
6) The isoelectric point determined by paper electrophoresis was about pH 4.7.
7) The ORD and CD spectra of RNase M were measured in acetate buffer (pH 5.0), in 8M urea and in 6M guanidine-HCl. The ORD and CD curves measured in acetate buffer were almost indistinguishable from those measured in 8M urea in the longer wavelength region.
8) Most of the phenolic groups in RNase M have an abnormally high pKa value of about 11.95, in acetate buffer and in 8M urea, but that in 6M guanidine-HCl is about 10.3.抄録全体を表示PDF形式でダウンロード (1263K) -
VI. Aromatic Amidines as Competitive Inhibitors of TrypsinKazutaka TANIZAWA, Shin-ichi ISHII, Kozo HAMAGUCHI, Yuichi KANAOKA1971 年 69 巻 5 号 p. 893-899
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリーThe effect of alteration of the aromatic hydrocarbon moiety of aromatic amidines on their inhibitory effects on trypsin [EC 3. 4. 4. 4] were investigated. β-Naphthamidine (Ki=6.6×10-8M) was slightly more inhibitory than benzamidine, suggesting that the former interacts more effectively with the “hydrophobic site” of the enzyme. In sharp contrast, however, α-naphthamidine was distinctly less inhibitory (Ki=2.4×10-4M) than the, β-derivative. This difference is interpreted in terms of the shape of the “slit” at the active center of trypsin which accommodates the hydrophobic part of the inhibitor molecules. The bindings of α- and β-naphthylmethylamines were similar. In addition to kinetic assays, the circular dichroic spectra were examined and gel filtration techniques were employed to examine the interaction btween trypsin and β-naphthamidine.抄録全体を表示PDF形式でダウンロード (467K) -
Hiroh IKEZAWA, Kimiko IKEZAWA, Yuji TONOMURA, Manuel F. MORALES1971 年 69 巻 5 号 p. 901-907
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリー1. For the purpose of detection of the intermediate E-OP in the reaction of myosin-ATPase [EC 3. 6. 1. 3], the possibility of back-incorporation of 14C from labelled ADP into ATP was examined. The main project was to confirm the reverse reaction, ADP+E-OP→ATP+E, by deceleration of the hydrolytic process, E-OP→E+Pi, with D2O.
2. Myosin-ATPase was incubated at 25°C with ATP and 14C-labelled ADP in the medium of D2O (pD 8.0). The mixture of the reaction products was desalted by a Sephadex G-10 treatment, and chromatographed on Dowex 1-X4, yielding three nucleotide fractions, i.e., AMP, ADP and ATP. The specific activities of three nucleotide fractions were calculated based on the radioactivities of these fractions determined by a scintillation counter.
3. After a prolonged incubation, a small amount of 14C was incorporated from ADP into ATP. However, an additional experiment showed that this back-incorporation was explainable as due to the action of myokinase [adenylate kinase, EC 2. 7. 4. 3], which was a contaminant in the myosin preparation.
Thus a phosphorylated myosin, E-OP, is not demonstrable by this method.抄録全体を表示PDF形式でダウンロード (469K) -
XIX. On the Subunit Structure and Spin States of Cytochrome Oxidase from Beef Heart MuscleToshihiro TSUDZUKI, Kazuo OKUNUKI1971 年 69 巻 5 号 p. 909-922
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリー1. As shown already by Orii and Okunuki (1), cytochrome oxidase** [EC 1. 9. 3. 1] prepared by the method devised by Okunuki et al. (2) existed in an aggregated state. Enzymatic activity of the oxidase was activated by sodium dodecyl sulfate at low concentration as a result of depolymerization of the original enzyme with s20, w of 22-23-S to the 16-17-S and 6-7-S components. The 16-17-S component had much higher specific activity than that of the original one, but further activation was not observed by additional action of SDS. PCMB facilitated dissociation of the 16-17-S (dimer per heme a) component to the 6-7-S one in the presence of SDS and simultaneously removed the copper from the oxidase. These results are compatible with the view that the functional unit of the oxidase contains two heme a molecules in it in an unseparable fashion.
2. Under alkaline conditions the presence of rapidly and slowly reducible components were suggested from spectroscopic observations made in the Sorect band region. Only the latter component seemed to react with carbon monoxide. Behavior of the 830-mμ band of the enzyme coincided well with that of the rapidly reducible one, indicating that the 830-mμ band was independent of the chromophore(s) of the CO-binding component (3, 4).
3. From the EPR studies carried out at 20°K, it became apparent that the enzyme contained two sorts of low spin hemes a (gx=1.55, gy=2, gx=3.01 and gy=1.88, g_??_=2, 26, g_??_=2.54) in fairly comparable amounts and a few amount of high spin heme a (ca. 20% of the total heme a). In the oxygenated enzyme, most of the essential copper and a considerable amount of low spin heme a with g=3.01 were in oxidized state. The result showed that change of the copper valence was synchronized with the redox-behavior of the 830-mμ p band, and that the reduced copper was more easily oxidized by aeration than the ferrous heme a component with g=3.01.
4. Measurement of the paramagnetic susceptibility from 273°K to 77°K revealed that there was no thermal change in the spin state of heme a of cytochrome oxidase contrary to the suggestion by Ehrenberg and Yonetani (5), so that if one low spin heme a is exchangeable to the high spin state, as shown by van Gelder et al. (6), the exchanging mechanism should be sought in other factors such as conformational changes in the enzyme molecule.抄録全体を表示PDF形式でダウンロード (887K) -
I. Effect of Cold-exposure on GluconeogenesisHachiro NAKAGAWA, Katsuya NAGAI1971 年 69 巻 5 号 p. 923-934
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリーKey gluconeogenic enzymes in rat liver markedly increased after a short period of cold-exposure. The activity of phosphoenolpyruvate carboxykinase [EC 4.1.1.32] showed a diurnal variation with the highest value at 7 pm and the lowest at 10 am in rats maintained at room temperature, but the activity exceeded the value of control group after 3 hr cold-exposure. The activity of serine dehydratase [EC 4. 2. 1. 13] did not vary diurnally in animals on a 25% casein diet and significantly increased after 12 hr exposure to cold.
In contrast to these key gluconeogenic enzymes, key glycolytic enzymes in the liver, such as pyruvate kinase [EC 2. 7. 1. 40] and key lipogenic enzymes, such as malic enzyme [EC 1. 1. 1. 38] and glucose-6-phosphate dehydrogenase [EC 1. 1. 1. 49] decreased in activity on exposure to cold, but the changes in their activities oc-curred much slower than those of the key enzymes of gluconeogenesis. Significant decreases in their activities were observed after 72 hr cold-exposure.
The physiological meaning of the changes in these enzyme activities in response to cold was also investigated on nutritional and enzymological bases after 8 day cold-exposure, when these enzymatic changes were firmly established and moreover shivering thermogenesis was considered to be still actively working. In consistency with the marked activation of serine dehydratase, cold-exposure increased the urea concentration in the liver and blood plasma as well as the ratio of the mean food intake to mean body weight gain on 12.5% and 25% casein diets. This suggests that protein or amino acids are utilized as sources of gluconeogenesis even in animals on a carbohydrate-rich diet (e. g. 78.4% carbohydrate, in the 12.5%, casein diet).
Comparison of the amounts of nitrogen ingested and the activation of key enzymes of gluconeogenesis in animals maintained on a complete amino acid-diet and those on a 12.5% casein diet suggested that amino acids may be better sources for gluconeogenesis than protein.
Cold-exposure produced significant increases in activities of hexokinase [EC 2. 7. 1. 1] and phosphofructokinase [EC 2. 7. 1. 11], but caused no change in the activity of pyruvate kinase in skeletal muscle.
Thus, the changes of key gluconeogenic enzymes in the liver are similar to those of key glycolytic enzymes in skeletal muscle, and not similar to those of key glycolytic enzymes in liver. These findings suggest that the increased gluconeo-genesis in response to cold supplies glucose as a heat source for shivering muscles.抄録全体を表示PDF形式でダウンロード (757K) -
Kazuko SEKIYA, Yuji TONOMURA1971 年 69 巻 5 号 p. 935-950
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリーActo-H-meromyosin was reconstituted from H-meromyosin and a preparation of F-actin prepared by extraction at room temperature, i.e. a complex of F-actin and regulatory proteins. The effects of Ca2+ and of modification of H-meromyosin with CMB on the acto-H-meromyosin-ATP system in 2 mM MgCl2, 50mM KCl and 20mM Tris-maleate at pH 7.0 and 21-25° were investigated. The following results were obtained.
1. On adding ATP to acto-H-meromyosin, its intensity of light-scattering decreased to the level of the suns of those of H-meromyosin and F-actin. The value of τ1/2 (the time for half the final decrease in light-scattering) was about 0.2 sec when 10 pM ATP was added, and decreased with increasing ATP concentration. It was unaffected by adding 0.1 mM CaCl2 or 0.1 mM EGTA. The value of τ1/2 for the recovery from the reduced scattering intensity was about 8 sec, and was unaffected by adding CaC12 or EGTA. The binding of H-meromyosin with F-actin was complete within 0.5 sec and was independent of Ca2+
. 2. One mole of initial burst of Pi-liberation was observed per mole of H-meromyosin, when 10 μM ATP were added to acto-H-meromyosin. The initial burst of P;-liber-ation was complete within 0.2 sec. At ATP concentrations below 3 PM, the acto-myosin type ATPase [EC 3. 6. 1. 3] activity in the steady state increased with in-creasing ATP concentration, and was independent of Ca2+. At ATP concentrations above 3 μm, the activity decreased with increasing ATP concentration. The inhi-bition by excess substrate was much greater in the presence of EGTA than in the presence of Ca2+.
3. The ATPase activity of acto-H-meromyosin, which was reconstituted from H-meromyosin and purified F-actin, was independent of Ca2+, but was inhibited by substrate at concentrations above 3 μM. The actomyosin type ATPase activity in-creased with increase in F-actin concentration. The maximum activities, obtained by extrapolating F-actin concentrations to infinity, were almost independent of the methods of preparation of actin and treatment of H-meromyosin with CMB and β-mercaptoethanol.
4. The initial rate of decrease in light-scattering of acto-H-meromyosin induced by ATP was reduced to one third of the control value by treatment of H-meromyosin with CMB and β-mercaptoethanol. The extent of decrease in light-scattering of acto-H-meromyosin after this treatment induced by a sufficient amount of ATP was about 60% of that of untreated acto-H-meromyosin. In the steady state the rate of ATP hydrolysis by acto-H-meromyosin reconstituted from F-actin and CMB-treated H-meromyosin was independent of Cat+, and increased monotonously with increasing ATP concentration.
5. These results were analyzed by the following reaction mechanism for the acto-H-meromyosin-ATP system:
_??_
where ks, and KD are the rate constants and the dissociation constants, respectively, of the steps indicated. S and RP-FA-HMM represent, respectively, substrate (ATP) and acto-H-meromyosin reconstituted from F-actin extracted at room temperature (a complex of F-actin, FA, with regulatory proteins, RP) and H-meromyosin (HMM)._??_is a complex of RP-FA with phosphoryl H-meromyosin, which_??_is formed by the reaction of H-meromyosin with ATP, and RP-FA-HMM:_??_is a complex of RP-FA with a H-meromyosin-phosphate-ADP complex which is formed via RP-FA-HMM_??_and rapidly dissociates into RP-FA and HMM:_??_with a dissociation constant KD', which is much larger than KD. The actomyosin type ATPase reaction takes place via two routes: steps 3 and 5. The following con-clusions were deduced from the above results. The formation of phosphoryl-H-meromyosin (step 1, 2) is independent of the presence of F-actin, regulatory proteins or Ca2+抄録全体を表示PDF形式でダウンロード (4673K) -
I. Purification and Properties of a Ribonuclease from Horse Submaxillary GlandSeiyu HIROSE, Kazuei IGARASHI, Tsuneko NABA, Yasuyo TSUDA, Akira MINAT ...1971 年 69 巻 5 号 p. 951-963
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリー1. A ribonuclease (H. S. RNase) was extracted from horse submaxillary gland with isotonic KCl and purified about 15, 000-fold with an over-all yield of about 14%.
2. The enzyme was free of DNase [EC 3. 1. 4. 5], nonspecific phosphodiesterase [EC 3. 1. 4. 1] and phosphomonoesterase [EC 3.1.3.1] activities, and appeared homogeneous on ultracentrifugation, paper electrophoresis, CM-cellulose column chromatography and gel filtration.
3. The mode of action of H. S. RNase on RNA was found to be similar to that of RNase A* [ribonucleate pyrimidinenucleotido-2'-transferase (cyclizing), EC 2. 7. 7. 16]. However, the base specificities of H. S. RNase and RNase A differed the former exhibiting little if any preference for cytosine over uracil in the degradation of 2', 3'-cyclic nucleotides and RNA at pH 8.3.
4. H. S. RNase was found to differ from RNase A in molecular weight estimated by a Sephadex gel filtration method (H. S. RNase: ca. 24, 000), specific activity (H.S. RNase: RNase A=1:2), elution position from a CM-cellulose column, and resistance to inhibition by heparin. Small but significant differences were also observed in the isoelectric points and pH optima of these enzymes.
5. H. S. RNase is very similar to RNase A in its heat stability and inhibition by Zn2+, Cd2+, Cu2+ and Hg2+.抄録全体を表示PDF形式でダウンロード (1497K) -
Masachika IRIE1971 年 69 巻 5 号 p. 965-968
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (237K) -
Tetsuro YOSHIMURA, Toshizo ISEMURA1971 年 69 巻 5 号 p. 969-972
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (970K) -
Hirotsugu TAKAHASHI, Etsuko SATO, Kiyoshi KURAHASHI1971 年 69 巻 5 号 p. 973-976
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (259K) -
Mitsuo SAITO, Tyunosin UKITA1971 年 69 巻 5 号 p. 977-981
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (221K) -
Koscak MARUYAMA, Sumiko KIMURA1971 年 69 巻 5 号 p. 983-985
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリーEffect of α-actinin, the Z band-constituting protein, on the tension development of surface-spread actomyosin fibers was investigated. α-Actinin remarkably enhanced contraction of actomyosin fibers made from myosin and pure F-actin. However, actomyosin fibers containing no a-actinin significantly developed tension upon addition of MgATP.抄録全体を表示PDF形式でダウンロード (136K) -
Tairo OSHIMA, Kazutomo IMAHORI1971 年 69 巻 5 号 p. 987-990
発行日: 1971/05/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (249K)
- |<
- <
- 1
- >
- >|