泥蚶体液和肌肉提取液凝集素的初步研究

利用14种天然或经酶修饰的动物及人红细胞来测定泥蚶的体液和肌肉提取液的凝集活力,并且进行糖(200 mmol·L-1)抑制、热稳定性、pH及Ca2+ 影响试验.结果显示:泥蚶体液和肌肉提取液对14种红细胞均有凝集作用.体液对兔红细胞的凝集作用可被乳糖和半乳糖所抑制,其凝集活性依赖于Ca2+,在pH7.0较稳定,经90 ℃保温10 min后活性完全消失;肌肉提取液的凝集活性不被实验所用的10种糖所抑制,在pH6.0~7.0,温度为60 ℃~90 ℃范围内均具较高活性,其凝集活性也依赖于Ca2+.推测:泥蚶的体液与肌肉提取液均含有凝集素,且种类不同.     

拟穴青蟹凝集素的活性及其部分性质

采用生物化学的方法研究了拟穴青蟹凝集素的部分性质,结果表明：拟穴青蟹血清的凝集素可凝集兔子、鸽子、鸭子、鸡的动物血红细胞,并且对不同的红细胞的凝集效价有所不同,该凝集素的活性受D-半乳糖、麦芽糖、鼠李糖等3种糖所抑制.在温度为30～40℃,pH为7.0,盐度为24时,拟穴青蟹血清凝集素活性最高.拟穴青蟹血清样品的凝集素受Ca2＋的依赖性较小.     

鲫鱼肌肉细胞核糖体酸性蛋白的分离与纯化

本文报导了一种分离纯化鲫鱼肌肉细胞核糖体酸性蛋白质的方法,并测得其亚基分子量约为12.400道尔顿。为今后的序列测定提供了基础。     

乳酸脱氢酶的分离纯化及其性质的研究

乳酸脱氢酶是在厌氧条件下能够催化丙酮酸接受NADH上的氢,生成乳酸;当动物体体内缺乏葡萄糖时,还可以氧化乳酸生成丙酮酸并经葡萄糖异生途径转变为葡萄糖的一组同工酶．蛋白质的分离纯化是研究蛋白质的结构与功能的一种有效手段．现已有大量的关于LDH分离纯化及其性质研究的文献报道,本文将其综述如下．     

来自链霉菌属的阿魏酸酯酶的分离纯化、理化性质

通过盐析透析、离了层析、疏水层析,对链霉菌属发酵液中的阿魏酸酯酶（FAE）进行分离纯化。并进行酶学性质研究。得出的阿魏酸酯酶的纯化倍数为2．67,回收率为55．8％,酶分子约为30kDa。其最适反应pH约为6．0,最适温度约为50℃,金属离子Cu^2＋和Zn^2＋对阿魏酸酯酶酶活力均有明显的抑制作用,而Mg^2＋、Fe^2＋、Ca^2＋、Na^＋和Mn^2＋对酶的活性均有一定的促进作用。     

黑曲霉糖化酶分离纯化与酶学性质研究

纯化了黑曲霉Aspergillus niger FJL0801糖化酶,并对其酶学性质进行研究.粗酶液经纯化后,较粗酶液纯化了38.42倍,酶活回收率达到17.45%.酶最适作用温度为60℃;最适反应pH值为4.5;在60℃下,保温2 h后,相对酶活42%±2.8%.在pH4.5,60℃下,作用时间在60 min以内,其酶活保存89%±2.56%;其酶学性质符合淀粉糖化工业化过程中对酶的要求,该酶比较适合应用于淀粉糖化工业.     

黄粉虫几丁质酶的纯化及性质

以黄粉虫为材料,采用盐析、亲和柱层析、Sephadex G-100分子筛及DE-52离子交换柱层析等制得纯化倍数约33倍,回收率为38%,比活力为294.7U/mg的几丁质酶制剂.在此基础上,以胶体几丁质为底物,考察黄粉虫几丁质酶的性质.结果表明：该酶催化水解几丁质的Km值为71.4mg/L;酶的最适pH值是6.0;最适温度为45℃左右;酶在pH 5.0～7.0,45℃以下酶活力稳定性较好.Na＋和K＋对酶活无影响;Ca2＋、Cu2＋对酶活起先扬后抑作用;Mn2＋、Mg2＋、Fe3＋、Al3＋对该酶活力均具有不同程度的抑制作用.     

不同植物材料中SOD的初步纯化及性质

以大蒜、芦荟为实验材料,采用热变性结合硫酸铵分段盐析法进行SOD的初步纯化,并对其SOD的部分性质做了研究.结果表明:大蒜和芦荟SOD的最终纯化倍数分别为6.2和3.3,活力回收率分别为55%和46%,最适温度分别为40℃和45℃,最适pH值分别为7.0和9.0.两者SOD均有较好的热稳定性.     

罗氏沼虾血清及肌肉提取液凝集活性的比较研究

用12种天然或经酶修饰的动物及人红细胞测定罗氏沼虾的血清和肌肉提取液的凝集能力，同时进行糖抑制、热稳定性、pH及Ca^2＋影响试验．结果显示，罗氏沼虾血清对鹤鹑红细胞的凝集效价比肌肉提取的高，且糖抑制、热稳定性、pH适应范围及对Ca^2＋的依赖性都存在明显差别．表明罗氏沼虾血清和肌肉提取液所含凝集素的类型不同．     

Purification and some properties of a β-glucanase from a strain, Trichoderma reesei GXC

β-glucanase was purified from a solid-state culture of Trichoderma reesei on wheat bran in three steps which comprised ammonium sulfate precipitation, Sephadex G-100 chromatography, and DEAE-Sephadex A-50 chromatography. The molecular mass was determined to be 35.21 kilodaltons by sodium dodecyl sulfate-12.5% polyacrylamide gel electrophoresis. The β-glucanase at low pHs was more stable than that at high pHs, and optimum pH was 5.0. The optimum temperature was 60 ℃, and β-glucanase was relatively stable at below 40 ℃ for 60 min. The Km of the enzyme on β-glucan was 10.86 mg/ml, and the Vmax on β-glucan was 14286 μmol of glucose equivalents per mg of the pure enzyme per min. The β-glucanase activity was significantly inhibited by Fe3+ ions, and was reduced in the presence of Cu2+ ions, Mn2+ ions and Mg2+ ions at 5 mmol/L and 10 mmol/L, respectively. The β-glucanase activity was stimulated by Co2+ ions, Ca2+ ions, Zn2+ ions, and Fe2+ ions at 1 mmol/L and 5 mmol/L, respectively.     

Burkholderia cepecia.njut01中D-海因酶和D-N-氨甲酰-氨基酸酰胺水解酶的纯化和性质

Abbreviation　　BH: 5 benzylhydantoin,　MH: 5 methyl hydantoin,　HPH: 5 (4 hydroxyphenyl) hydantoin,　MTEH: 5 (2’ methylthioethyl) hydantoin,　IPH: 5 isopropylhydantoin,　Nphe: N Carbamoyl phenylalanine,　Nala: N Carbamoyl alanine,　NHPG:N Carbamoyl p hydroxyphenylglycin,　Nval: N carbamoyl Valine.1　Introduction　Optically active D amino acids are widely used forthe production of semisynthetic antibiotics, antifungalagents, pesticides, hormones and sweeteners. There isa…     

Purification and Biochemical Characterization of D-hydantoinase and D-N-carbamoylase from Burkholderia cepecia, njut01

Hydantoinase and N-carbamoylase play important roles in the production of optically pure amino acids from racemic 5-monosubstituted hydantoins. In this report, hydantoinase and the N-carbamoylase from Burkholderia cepecia, njut01 were purified to homogeneity by chromatography (Pharmacia Explorer 100 system). The substrate specificity, enantioselectivity, pH dependence of activity and temperature stability of the activity were characterized. The results show that the hydantoinase and N-carbamoylase induced from Burkholderia cepecia, njut01 are both strict D-stereo selective enzymes. They both hydrolyze substrates with side chains containing aliphatic and aromatic residues with higher activity and affinity toward aromatic than aliphatic substituted substrates. The hydantoinase is a homotetramer with subtmit molecular weight near 52,000 and is active between pH 6.5 and 10 with an optimum near pH 9.0. The enzyme is active at temperatures up to 60~C, however, it appears instable at higher temperatures. The subunit molecular weight of N-carbamoylase is about 35KD. The N-carbamoylase is active in the pH range from 6.0 to 9.5. The optira-pH is 7.2 and the optinfizing bioconversion temperature of the N-carbamyolase is 52℃.     

不同的理化因素对糯米凝集素活性的影响

凝集素是一种能使血细胞发生凝集的糖蛋白,同时又是食品中的抗营养因子,其凝集活性受多种因素影响.本文研究不同的理化因素对糯米凝集素活性的影响,以便提高食物的安全性.     

蒜头果蛋白的提取及凝血活性测定

从云南、广西濒危植物蒜头果中分离、纯化出一种新的蛋白质―蒜头果蛋白,并分别用鸡、兔的红细胞悬液检测其凝血活性.结果表明,蒜头果蛋白对鸡、兔的红血球都具有凝集作用,是一种凝集素,有开发利用价值.     

社区体育活动中的健身健美方法

文章讨论了社区体育活动中易学、易练、易掌握的六种健身健美方法,和发达不同部位肌肉的练习方法.对健美体型、增强肌力、提高器官机能、培养良好的审美意识和陶冶情操有重要作用.     

Purification and some properties of a β-glucanase from a strain,Trichoderma reesei GXC

β-glucanase was purified from a solid-state culture ofTrichoderma reesei on wheat bran in three steps which comprised ammonium sulfate precipitation, Sephadex G-100 chromatography, and DEAE-Sephadex A-50 chromatography. The molecular mass was determined to be 35.21 kilodaltons by sodium dodecyl sulfate-12.5% polyacrylamide gel electrophoresis. The β-glucanase at low pHs was more stable than that at high pHs, and optimum pH was 5.0. The optimum temperature was 60°C, and β-glucanase was relatively stable at below 40°C for 60 min. TheK _m of the enzyme on β-glucan was 10.86 mg/ml, and theV _max on β-glucan was 14286 μmol of glucose equivalents per mg of the pure enzyme per min. The β-glucanase activity was significantly inhibited by Fe³⁺ ions, and was reduced in the presence of Cu²⁺ ions, Mn²⁺ ions and Mg²⁺ ions at 5 mmol/L and 10 mmol/L, respectively. The β-glucanase activity was stimulated by Co²⁺ ions, Ca²⁺ ions, Zn²⁺ ions, and Fe²⁺ ions at 1 mmol/L and 5 mmol/L, respectively. Project supported by Foundation for University Key Teacher of the State Ministry of Education, the National Natural Science Foundation of China (No. 30000118) and Zhejiang Provincial Natural Science Foundation of China (No. 399409).