期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1971
卷号：68
期号：6
页码：1226-1230
DOI：10.1073/pnas.68.6.1226
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Two new forms of carboxypeptidase B have been isolated from spontaneously activated bovine pancreatic juice. The fully active enzymes contain an internal split at residues 92-93 and 95-96, respectively. Sequenator analysis of the amino terminal segments of the two chains of the enzyme has extended the sequence information by 51 amino acid residues. Comparison of 125 residues strengthens the hypothesis that carboxypeptidases A and B are homologous both in amino acid sequence and in three-dimensional conformation and implicates Asp-255 as the anionic site of substrate binding of the B enzyme.
关键词：amino acid sequence ; active site ; proteolytic cleavage
