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T Ishii H Iwahashi R Sugata R Kido I Fridovich 《Archives of biochemistry and biophysics》1990,276(1):248-250
The autoxidation of 3-hydroxyanthranilate to cinnabarinate at 37 degrees C and at pH 7.4 is hastened by superoxide dismutase (SOD). The Cu,Zn-containing enzyme from bovine erythrocytes and the Mn-containing enzyme from Escherichia coli were equally effective in this regard; whereas the H2O2-inactivated Cu,Zn enzyme was ineffective. Catalase appears to augment the effect of superoxide dismutase, because it prevents the bleaching of cinnabarinate by H2O2. It follows that O2-, which is a product of the autoxidation, slows the net autoxidation by engaging in back reactions and that SOD increases the rate of autoxidation by removal of O2- and thus by prevention of these back reactions. 相似文献
23.
Inhibition of rabbit liver fructose 1,6-biphosphatase by AMP: effect of temperature and physiological concentrations of cations and anions 总被引:2,自引:0,他引:2
A Vita H Kido S Pontremoli B L Horecker 《Archives of biochemistry and biophysics》1981,209(2):598-605
Turkey gizzard smooth muscle myofibrils, the actin of which is composed of 75% smooth muscle γ-isoactin and 25% nonmuscle β-isoactin, were separated into an actomyosin and a cytoskeletal fraction. Isoelectric focusing analysis of the actomyosin actin showed it was 80% γ-isoactin and 20% β-isoactin. It thus appears that the major actin in the tissue is also the major form involved in force generation. When the cytoskeletal material was extracted with low-ionic-strength solution for 18 h at 4 °C, the actin released was 95% γ and 5% β compared with the 75:25 ratio found in the original cytoskeletal material. The extracted material revealed the presence of F-actin filaments and high-molecular-weight aggregates. Little of the material was in a low-molecular-weight form. On the other hand, extraction of the cytoskeletal material with 0.6 m KI resulted in the two isoactins being extracted in the same proportions in which they were found in the original cytoskeletal material. However, when this KI-extracted material was subsequently chromatographed on Bio-Gel A-5m equilibrated with 0.6 m KCl, the γ-isoactin migrated predominantly as a very high molecular weight form while the β-isomer moved in the lower-molecular-weight range of the elution profile. This aggregation behavior displayed by the γ-isoactin was not observed with the γ-isoactin in the actomyosin fraction. These results show that the two gizzard isoactins in the cytoskeletal residue behave very differently in response to various extraction media, and are consistent with possible differential isoactin utilization in gizzard smooth muscle. 相似文献
24.
Kynurenine pyruvate aminotransferase was purified from rat kidney. The purified enzyme had an isoelectric point of pH 5.2 and a pH optimum of 9.3. The enzyme was active with pyruvate as amino acceptor but not with 2-oxoglutarate, and utilized various aromatic amino acids as amino donors. L-Amino acids were effective in the following order of activity: histidine greather than phenylalanine greater than kynurenine greater than tyrosine greater than tryptophan greater than 5-hydroxytryptophan. The apparent Km values were about 0.63 mM, 1.4 mM and 0.09 mM for histidine, kynurenine and phenylalanine, respectively. Km values for pyruvate were 5.5 mM with histidine as amino donor, 1.3 mM with kynurenine and 8.5 mM with phenylalanine. Kynurenine pyruvate aminotransferase activity of the enzyme was inhibited by the addition of histidine or phenylalanine. The molecular weights determined by gel filtration and sucrose density gradient centrifugation were approximately 76000 and 79000, respectively. On the basis of purification ratio, substrate specificity, inhibition by common substrates, subcellular distribution, isoelectric focusing and polyacrylamide-gel electrophoresis, it is suggested that kynurenine pyruvate aminotransferase is identical with histidine pyruvate aminotransferase and also with phenylalanine pyruvate aminotransferase. The physiological significance of the enzyme is discussed. 相似文献
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Toshiko Kido Katsuyuki Tanizawa Kenji Inagaki Tohru Yoshimura Masaaki Ishida Katsumi Hashizume 《Bioscience, biotechnology, and biochemistry》2013,77(10):2549-2554
2-Nitropropane dioxygenase, purified to homogeneity by an improved method from a yeast, Hansenula mrakii, has a molecular weight of 42,000, and consists of a single polypeptide. The enzyme contains 1 mol of FAD per mol of enzyme. The iron protein associated with previous preparations was removed by the present purification procedures. The enzyme catalyzes the oxygenative denitrification of anionic nitroalkanes much more effectively than that of the neutral ones with the optimum pH of 6.5. The Michaelis constants for the anionic substrates are as follows: 2-nitropropane, 1.61 mM; 1-nitropropane, 3.23 mM; nitroethane, 3.13 mM, and 3-nitro-2-butanol, 0.59 mM. 相似文献
28.
Motoo Shibata Masaru Uyeda Yutaka Kido Keiko Shigemori Yoko Aziki Toyoki Hirakawa 《Bioscience, biotechnology, and biochemistry》2013,77(9):1767-1771
From the results of taxonomic studies, Streptomyces sp. strain No. KT–151 isolated from a soil sample collected in Kumamoto City, was identified as a strain belonging to Streptomyces luteogriseus Schmitz, Deak, Crook and Hooper 1964. A new antibiotic, produced by this strain, was isolated as a leaflet crystal by ion-exchange chromatography and found to be an amino acid with the molecular formula, C5H12N2O2, and named antibiotic KT–151 (refered to as KT–151 hereinafter). The antibiotic showed antimicrobial activity against various Gram-positive and Gram-negative bacteria in a chemically defined medium but it was antagonized by several amino acids such as valine, leucine, isoleucine and threonine. 相似文献
29.
Miyagawa Eiji Junko Yano Toshinari Hamakado Yasuji Kido Keiji Nishimoto Yoshinobu Motoki 《Bioscience, biotechnology, and biochemistry》2013,77(10):2881-2886
N-Benzoylgiycine amidohydrolase (hippurate hydrolase EC 3.5.1.32), which catalyzes the hydrolysis of hippuric acid to benzoic acid and glycine, was found in a cell-free extract of Pseudomonas putida C692-3 grown on a medium containing hippuric acid. The enzyme was purified from the extract by ammonium sulfate fractionation and column chromatographies on DEAE-cellulose, DEAE-Sephadex A-50, hydroxyapatite, and Sepharose CL-6B. The enzyme was finally crystallized. The crystalline enzyme was almost homogeneous on electrophoresis. The enzyme had a molecular weight of about 170,000 and consisted of four subunits identical in molecular weight (approximately 42,000). The enzyme hydrolyzed N-benzoylglycine most rapidly, and N-benzoyl-l-alanine and N-benzoyl-l-aminobutyric acid. The Km value for these substrates were 0.72 mm, 0.87 mm, and 0.87mm, respectively. The optimum pH of the enzyme reaction was 7.0 to 8.0 and the enzyme was stable from pH 6.0 to 8.0. 相似文献
30.
Masayoshi Tabata Takahiro Kido Masayuki Totani Takashi Murachi 《Bioscience, biotechnology, and biochemistry》2013,77(7):1909-1910
(22R,23R,24S)-3α,5-Cyclo-22,23-diacetoxy-5a-ergostan-6-one (2b) is a new key intermediate of some naturally occurring brassinosteroids such as brassinolide (la), castasterone (lb), teasterone (lc) and typhasterol (Id). The cycloketone 2b was prepared in 10 steps via (22R,23R,24S)-6p- benzyloxy-3a,5-cyclo-22,23-dihydroxy-5a-ergostane (5) from stigmasterol. 2b was treated with a catalytic amount of /7-toluenesulfonic acid and sodium bromide to give an enone (7b), which was oxidized with osmium tetroxide and derived to give a 2a,3a-acetonide (8b). 8b was easily separated from its isomer by the use of silica gel column chromatography. 8b was oxidized with tri- fluoroperacetic acid and deacetylated to give la. 8b was deacetylated and deacetonized to give lb. 2b was treated with dilute sulfuric acid in acetic acid to give a 3/^-acetate (10). 10 was treated with sodium hydroxide to give lc. 2b was treated with hydrobromic acid to give a 3/i-bromide (12), which was treated with silver acetate to give a 3a-acetate (13). 13 was treated with sodium hydroxide to give Id. 相似文献