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M. M. Hernández-Herrero A. X. Roig-Sagués E. I. López-Sabater J. J. Rodríguez-Jerez M. T. Mora-Ventura 《European Food Research and Technology》2000,212(1):26-30
Changes in the muscle proteins during the ripening of salted anchovies have been examined using sodium dodecyl sulphate polyacrylamide
gel electrophoresis. The chemical changes occurring in the muscle proteins of anchovy during the ripening process were related
to the degradation of the myofibrillar structure of the muscle. In spite of a considerable protein degradation the ripened
salted anchovy maintained its structure and was easily cut into fillets. Hydrolysis of muscle proteins was significant during
the first 6 weeks. Proteins of molecular weight higher than 35 kDa were more likely to be hydrolysed. Myosin heavy chains
were the most sensitive myofibrillar protein. α-Actinin, actin and tropomyosin were more resistant to enzymatic degradation.
Due to protein build-up of peptides resulting from the breakdown of the higher molecular proteins, it was difficult to measure
changes in the myosin light chains and troponin sub-units.
Received: 28 December 1999 / Revised version: 9 March 2000 相似文献
94.
大豆脂肪氧化酶凝胶电泳分析研究 总被引:5,自引:0,他引:5
本文介绍利用SDS电泳、簿层等电聚焦电泳技术及激光光密度计扫描分析大豆脂肪氧化酶的方法,其中薄层等电聚焦电泳技术具有准确、快速、分辨率高的特点,并应用于53份大豆资源LOX同功酶缺失体的鉴定以及激光扫描定量测定酶带峰值面积,为在我国开展大豆脂肪氧化酶研究提供了鉴定技术。 相似文献
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A surface protein layer was found to be present in some Lactobacillus acidophilus strains. it could be visualized with electron microscopy and extracted with sodium dodecyl sulfate or guanidine hydrochloride. The protein was resistant to several proteolytic enzymes, but sensitive to pronase. Amino acid composition analysis revealed about 30% hydrophobic amino acids. Hydrophobicity study with a hexadecane partition assay demonstrated that the cells were hydrophobic and removal of the surface layer with pronase destroyed the hydrophobic nature of the cells. Several growth conditions studies were found to have little effect on synthesis of the surface protein. 相似文献
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研究了二巯基苏糖醇(DTT)、亚硫酸钠(Na2SO3)和半胱氨酸(Cys)对大豆胰蛋白酶抑制剂活性的影响。实验在温度80℃,pH7.5条件下反应,并以BAPNA为底物,采用改进的方法测定DTT对大豆蛋白酶抑制剂的钝化作用,最后用SDS-PAGE方法和凝胶排阻色谱法研究其蛋白酶钝化敏感性。通过改进的BAPNA法得出还原剂钝化大豆胰蛋白酶抑制剂由大到小顺序依次为:DTT>Na2SO3>Cys,并通过SDS-PAGE进一步证实了比色法得出的结论。而凝胶排阻色谱法说明了还原剂对大豆胰蛋白酶抑制剂作用使得抑制剂中二硫键被打断,抑制剂结构发生改变,有新的物质生成。所以,得出大豆胰蛋白酶抑制剂的稳定性与二硫键的存在有关。 相似文献
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C N Suman P Vincent Monteiro Geeta Ramachandra L Sudharshana 《Journal of the science of food and agriculture》1992,58(4):505-509
To assess the nutritional quality of Japanese barnyard millet ( JBN , Echinochloa frumentacea Link), its protein content, quality and digestibility were studied. The proximate composition of the millet resembles that of other millets/cereals. The protein content had a mean value of 36.7 g kg?1. Solubility fractionation showed glutelins to be the major storage protein (60.8%). Contents of phenolics and tannins were estimated and found to be low. The protein digestibility of JBN flours was high (84%). The digestibilities of the different protein fractions varied from 50.9% to 68.4% with pepsin and from 26.6 mg g?1 to 55.8 mg g?1 (α-amino N liberated) with trypsin. These differences have been discussed relative to differences in amino acid composition of the protein fractions as well as to the possible presence of antinutritional factors in the fractions. 相似文献
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