摘要
经亲和层析得到Ｂｓｐ６３Ｉ．用对氯汞苯甲酸、磷酸吡哆醛、２，３－丁二酮修饰该酶的巯基、赖氨酸、精氨酸残基，结果表明：这些基团均与该酶活性有关．动力学研究表明磷酸吡哆醛对酶的抑制是一种类反竟争性抑制．
Restriction endonuclease Bsp63I has been isolated and purified by affinity chromatography. The role of specific amino acid residues in Bsp63I was determined by chemical modification. Sulfhydryl groups were modified with p-chloromercuribenzoic acid,lysineresidues with pyridoxal-5'-phosphate(PLP)and arginine residues with 2, 3-butanedione. Theresults show that these residues are related to activity of Bsp63I. Dynamic analysis showsthat the type of PLP inhibition is analogous anticompetitive inhibition.
出处
《武汉大学学报（自然科学版）》
CSCD
1996年第2期237-240,共4页
Journal of Wuhan University(Natural Science Edition)
