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31.
Takehiko Yamamoto Junichi Kumada Teruo Sawai 《Bioscience, biotechnology, and biochemistry》2013,77(3):185-191
The purification of yeast invertase was attempted by application of the chromatographic method using Duolite C-10, a sulfonic acid cation exchange resin. This method was found to be extremely simple in process and significantly effective for the improvement of purity of the enzyme, compared with those other methods reported, hitherto. In the present paper, the procedure of the purification and some properties of the enzyme obtained thereby, are described, and some discussion of the implications is presented. 相似文献
32.
Daisuke Tsuru Heizo Kira Takehiko Yamamoto Juichiro Fukumoto 《Bioscience, biotechnology, and biochemistry》2013,77(9):856-862
The neutral protease of Bacillus amylosacchariticus was inactivated by low concentrations of several metal-chelating agents and the inactivated enzyme with EDTA restored its activity almost completely by the addition of Zn++ or Co++ and partially by Fe++ or Mn++, if these metal ions were added shortly after the EDTA-treatment. The native enzyme was found to contain 0.19% of zinc together with a significant amount of calcium. Parallel increase in specific activity and zinc content of enzyme preparation was observed throughout the purification procedure. The elution pattern of enzyme activity on a CM-cellulose column chromatography also completely coincided with that of protein-bound zinc. A zinc-free inactive enzyme was also reactivated by the addition of zinc or cobalt ions, clearly showing that the neutral protease of B. amylosacchariticus is a zinc mctalloenzyme. 相似文献
33.
Masaru Iizuka Yasuhiko Torii Takehiko Yamamoto 《Bioscience, biotechnology, and biochemistry》2013,77(12):2767-2772
An enzyme which released invertase from cell ghosts of Candida utilis was isolated in an electrophoretically pure state from “Zymolyase.” The molecular weight of the purified enzyme was estimated to be 5.8 × 104, and its isoelectric point was pH 6.9. The enzyme was stable in a pH range from 6.0 to 9.0, and the optimal pH for liberation of invertase from cell ghosts was around 6.0. The activity of the enzyme was competitively inhibited by glucose, mannose, and sucrose. Unlike the starting enzyme preparation, “Zymolyase,” the purified enzyme released invertase without making holes on the surface of the cell ghosts. Various tests were applied, but the specificity of the enzyme was not defined. 相似文献
34.
Kimikazu Itaya Juichiro Fukumoto Takehiko Yamamoto 《Bioscience, biotechnology, and biochemistry》2013,77(6):813-821
Some physical and chemical properties of urate oxidase (EC 1.7.3.3) isolated from the cells of Candida utilis were investigated. The molecular weight was estimated to be 1.2 × 105 by the equilibrium sedimentation and gel filtration methods. The isoelectric point was determined as 5.4 by the method of density electrofocusing. The enzyme showed a slight absorption at 410 mμ, and the absorbancy at this wave length was only 3% of that at 280 mμ. Contrary to urate oxidase from swine liver, the enzyme from yeast contained a negligible amount of copper, but it contained iron of nearly one atom per mole of the enzyme protein. The yeast urate oxidase was not inactivated by some chelators. However, it was easily inactivated with certain heavy metal ions such as Hg2+, and the inactivated enzyme was reactivated by the addition of thiols, indicating that the enzyme is a sulfhydryl enzyme. The inactivation of the enzyme with urea, on the other hand, was greatly accelerated by the addition of thiols, and some discussion was added to the results obtained. 相似文献
35.
Shigenori Emi Juichiro Fukumoto Takehiko Yamamoto 《Bioscience, biotechnology, and biochemistry》2013,77(12):1891-1898
Many strains of Bacillus subtilis were found to secrete several hemicellulolytic enzymes such as arabinoxylanase, galactomannanase, arabinogalactanase, etc. Chemical and enzymatic properties of certain strains of the bacterium were comparatively investigated. An arabinogalactanase was purified and obtained in a crystalline state. Its molecular weight and isoelectric point were estimated to be 3.7×104 and 8.39, respectively. The enzyme showed an optimal pH for reactions at 6.0, and was stable in a pH range of 5.0 to 9.5 at 30°C. It required no metallic ions for its activity and hydrolyzed soybean arabinogalactan, forming galactobiose as the main product. No liberation of arabinose was observed in the hydrolysate. Also, the enzyme did not attack coffee bean arabinogalactan. Some implications of the experimental results are discussed. 相似文献
36.
Daisuke Tsuru Heizo Kira Takehiko Yamamoto Juichiro Fukumoto 《Bioscience, biotechnology, and biochemistry》2013,77(3):330-335
Some physicochemical properties and amino acid composition of the alkaline protease of B. amylosacchariticus were determined. The molecular weight and sedimentation coefficient were estimated to be 22,700 and 2.89 s, respectively, and the amino terminal amino acid was identified to be alanine. The enzyme contained 15.9% of nitrogen and was composed of 220 residues of amino acid: lys6, his5, arg3, asp20, thr14, ser37, glu12, pro10, gly25 ala27 val20, met3, isoleu12, leu12, tyr9, phe2, try3 and amide ammonia16 The results indicate that protein nature and chemical properties of the alkaline protease presented here are distinct from those of alkaline proteases obtained from the other strains of B. subtilis, such as subtilopeptidase A, B and BPN’ 相似文献
37.
Yoshikazu Matsumura Toshihiro Nakanishi Masaru Iizuka Takehiko Yamamoto 《Bioscience, biotechnology, and biochemistry》2013,77(2):379-386
1. A trial test was attempted of complete hydrolysis of peptides and proteins into amino acids by enzymes. “Neutral proteinase” of Bacillus subtilis or “Alkalophilic proteinase” of a Streptomyces sp. was used for preliminary digestion of substrate, and a mixture of three aminopeptidases of Bacillus subtilis was employed for subsequent hydrolysis of proteinase digest.2. The oxidized insulin B chain was hydrolyzed completely by the method. Several proteins including enzymes which contained no or less cystine and cysteine were also hydrolyzed almost completely.3. On the other hand, certain glycoproteins were hydrolyzed to leave a few glycopeptides in which all glycomoieties of the proteins were retained. The implications of the results are discussed. 相似文献
38.
Nobutake Hamada Takehiko Yamamoto Juichiro Fukumoto 《Bioscience, biotechnology, and biochemistry》2013,77(3):306-313
The nucleic acid metabolism in washed cells of Bacillus subtilis was investigated with special reference to amylase formation of the bacterium. On incubation of the suspension of the washed cells, purines, pyrimidines and their related compounds were observed in the medium. However, in the medium of the cells incubated with a calcium chelater, where no amylase formation occurred, were detected adenosine- and guanosine-monophosphate in addition to those described above. The addition of a calcium chelater was also found to decrease the quantity of the nucleic acids being involved in the lysozyme-sensitive fraction of the bacterial cells, suggesting the possibility that the metabolism of nucleic acids in this fraction is closely related to amylase formation of the cells. 相似文献
39.
Nishinaka T Doi Y Hashimoto M Hara R Shibata T Harada Y Kinosita K Noji H Yashima E 《Journal of biochemistry》2007,141(2):147-156
We have developed two experimental methods for observing Escherichia coli RecA-DNA filament under a fluorescence microscope. First, RecA-DNA filaments were visualized by immunofluorescence staining with anti-RecA monoclonal antibody. Although the detailed filament structures below submicron scale were unable to be measured accurately due to optical resolution limit, this method has an advantage to analyse a large number of RecA-DNA filaments in a single experiment. Thus, it provides a reliable statistical distribution of the filament morphology. Moreover, not only RecA filament, but also naked DNA region was visualized separately in combination with immunofluorescence staining using anti-DNA monoclonal antibody. Second, by using cysteine derivative RecA protein, RecA-DNA filament was directly labelled by fluorescent reagent, and was able to observe directly under a fluorescence microscope with its enzymatic activity maintained. We showed that the RecA-DNA filament disassembled in the direction from 5' to 3' of ssDNA as dATP hydrolysis proceeded. 相似文献
40.
Uchii Kimiko Wakimura Kei Kikko Takeshi Yonekura Ryuji Kawaguchi Riho Komada Honoka Yamanaka Hiroki Kenzaka Takehiko Tani Katsuji 《Limnology》2022,23(1):49-56
Limnology - Gnathopogon caerulescens is an endangered but commercially important fish in Lake Biwa, Japan. The population size of G. caerulescens has drastically reduced in the past decades, and... 相似文献