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991.
Shunya Takahashi Takayuki Oritani Kyohei Yamashita 《Bioscience, biotechnology, and biochemistry》2013,77(10):2711-2718
The total synthesis of ( + )-methyI phaseate (2b) and its epimer (25) is described. The known β- ketoester (8), which was prepared from ( — )-/f-pinene (4), was converted to a key intermediate (5) via a 1, 4-dioxoester (7). The reaction of 5 with a lithium reagent of the acetylene TBDMS ether (6) in THF-HMPA at — 70°C afforded the desired acetylene alcohol (17) and its epimer (18) in high yields. 17 was transformed into ( + )-methyl phaseate (2b). From this synthetic work, the absolute configuration of natural ( — )-phaseic acid (2a) was confirmed. 相似文献
992.
Kozi Asada Masa-aki Takahashi Mieko Nagate 《Bioscience, biotechnology, and biochemistry》2013,77(2):471-473
Allosamidin, a product of Streptomyces sp. No 1713, inhibited Bombyx mori chitinase specifically in a competitive way with a Ki o f about 0.1 μm. The effect of allosamidin on chitinases from r Streptomyces griseus and Serratia marcescens was weaker, about 1/500 that on B. mori chitinase. Allosamidin did not inhibit yam chitinase, lysozymes of hen egg-white or human urine, or B. mori α-N-acetyl-d-glucosaminidase. The results suggest that allosamidin is a specific inhibitor of the insect chitinase. 相似文献
993.
994.
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997.
Shigeo Kawata Eiji Takahashi Yoshiyuki Takase Kanae Yokogawa 《Bioscience, biotechnology, and biochemistry》2013,77(12):2801-2808
d-Alanyl-(d)-meso-2,6-diaminopimelic acid endopeptidase was purified 47.4-fold with a yield of 40.5% from mutanolysin, which was partially purified from the cultural supernatant of Streptomyces globisporus 1829, by using ion exchange column chromatographies and a molecular sieve column. The purified enzyme was electrophoretically homogeneous. This enzyme had a molecular weight of 13,500 and an isoelectric point of pI 9.0. This enzyme was most active at pH 8.5 and stable between pHs 8.0 and 9.0. The hydrolyzing activity of this enzyme was enhanced by Co+ + and Ca+ + but inhibited appreciably by Zn+ +, Cu+ + and EDTA. The enzyme activity was not affected by β-lactam antibiotics and vancomycin. The Km values for bisdisaccharide heptapeptide and its derivative modified chemically by BOC-S were calculated to be 5.7 × 10-4 and 4.0 × 10-4 m, respectively. 相似文献
998.
Nobutaka Takahashi Akinori Suzuki Satoshi Miyamoto Rinpei Mori Saburo Tamura 《Bioscience, biotechnology, and biochemistry》2013,77(8):583-589
Molecular formula C25H37–39NO4 was assigned to Piericidin A. Through the examination of the ultraviolet, infrared and n.m.r. spectra and of chemical evidences, it was shown that Piericidin A contains one secondary alcohol, one acidic hydroxyl group, two methoxyl groups, tri- and tetra-substituted conjugated dienes and one polysubstituted heteroaromatic ring. 相似文献
999.
Koshi Arai Tetsu Ando Akira Sakurai Hideo Yamada Tatsuo Koshihara Nobutaka Takahashi 《Bioscience, biotechnology, and biochemistry》2013,77(9):2395-2397
Gibberellins A4 and A36 were identified from flowering and vegetative apices of ten month-old sugarcane (Saccharum spp. hybrids) plants. The identifications were based on retention times, relative to authentic standards, on sequential silica gel partition column chromatography→bioassay→C18 reverse phase high performance liquid chromatography→bioassay→ capillary gas chromatography (GC), and on GC-selected ion monitoring (SIM), the relative intensities of six characteristic ions being monitored in comparison with authentic standards. 相似文献
1000.
Hirokazu Matsui Seiya Chiba Tokuji Shimomura Nobuyuki Takahashi 《Bioscience, biotechnology, and biochemistry》2013,77(11):2239-2240
Hen lysozyme modified with histamine (HML) and Japanese quail lysozyme (JQL) were treated with immobilized metal ion affinity chromatography to analyze the states of their imidazole groups. When Ni(II) was used as the metal ion immobilized, JQL was strongly retained in a Ni(II)-chelating Sepharose column, while hen lysozyme and HML were hardly retained in the same column. All of these lysozymes have a histidine imidazole group at the 15th position, while JQL has an additional histidine imidazole group at the 103rd position and HML has an additional imidazole group covalently attached to Asp101. Thus, I concluded that the imidazole group at the 103rd position of JQL is exposed to the solvent and recognized by the metal ion, but that the imidazole group attached to Asp101 in HML is localized to a hydrophobic region and not recognized by the metal ion. 相似文献