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粘质赛氏菌胞外蛋白酶的化学修饰
引用本文:潘继承,汪劲松,向显智,黄阜峰.粘质赛氏菌胞外蛋白酶的化学修饰[J].中国生物化学与分子生物学报,1997,13(4):483-486.
作者姓名:潘继承  汪劲松  向显智  黄阜峰
作者单位:湖北师范学院生物系
摘    要:用九种化学修饰剂研究了粘质赛氏菌SerratiaMarcescens41003(2)胞外蛋白酶分子中氨基酸侧链基团与酶催化活性的关系,结果表明组氨酸、丝氨酸、赖氨酸、精氨酸、谷氨酸及天冬氨酸等残基与酶活性无关;半胱氨酸残基与酶活性也无直接关系;而酪氨酸和色氨酸残基侧链的修饰引起酶活力大幅度下降,说明酪氨酸和色氨酸残基为酶活力必需.

关 键 词:粘质赛氏菌胞外蛋白酶  化学修饰  
收稿时间:1997-08-20

Chemical Modification of a Proteinase from Serratia Marcescens
Pan,Ji,Cheng,Wang,Jin,Song,Xiang,Xian,Zhi,Huang,Fu,Feng,.Chemical Modification of a Proteinase from Serratia Marcescens[J].Chinese Journal of Biochemistry and Molecular Biology,1997,13(4):483-486.
Authors:Pan  Ji  Cheng  Wang  Jin  Song  Xiang  Xian  Zhi  Huang  Fu  Feng  
Affiliation:(Department of Biology,Hubei Normal University,Huangshi 435002)
Abstract:The effects of protein modification reagents on the activity of the extracellular proteinase from Serratia Marcescens41003(2) have been studied.The proteinase was not affected by BAA,PCMB,TPCK,EDC,2,3 Diacetyl and DFP modification,indicating that thiol groups,carboxyl groups,histidine residues,lysine residues and arginine residues were non essential to enzyme activity.The enzyme activity was remarkably decreased after N AI,NBSF and NBS modification.The results indicated that tyrosine and tryptophane residues seemd to be essential to the catalytic activity of the proteinase.
Keywords:
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