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．
The effects of protein modification reagents on the activity of the extracellular proteinase from Serratia Marcescens41003(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.
关键词
粘质赛氏菌
胞外蛋白酶
化学修饰
Extracellular proteinase from Serratia Marcescens 41003(2),Chemical modification
