Abstract:
: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.
journal_name
Proc Natl Acad Sci U S Aauthors
Reeck GR,Walsh KA,Hermodson MA,Neurath Hdoi
10.1073/pnas.68.6.1226subject
Has Abstractpub_date
1971-06-01 00:00:00pages
1226-30issue
6eissn
0027-8424issn
1091-6490journal_volume
68pub_type
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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更新日期:2014-02-18 00:00:00
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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更新日期:1998-03-03 00:00:00