AMINO ACID SEQUENCE OF BOVINE CARBOXYPEPTIDASE A .2. TRYPTIC AND CHYMOTRYPTIC PEPTIDES OF CYANOGEN BROMIDE FRAGMENT F3

被引：36

作者：

BRADSHAW, RA

BABIN, DR

NOMOTO, M

SRINIVASIN, NG

ERICSSON, LH

WALSH, KA

NEURATH, H

机构：

[1] Department of Biochemistry, University of Washington, Seattle, Washington

来源：

BIOCHEMISTRY | 1969年 / 8卷 / 09期

关键词：

D O I：

10.1021/bi00837a052

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An 81 amino acid residue fragment (FIII) of bovine carboxypeptidase A, obtained by cleavage with cyanogen bromide and isolated by gel filtration on Sephadex G-75, has been subjected to tryptic and chymotryptic hydrolysis. The resulting peptides have been isolated and characterized by Edman degradations and hydrazinolysis, and by hydrolysis with carboxypeptidase A and B and leucineaminopeptidase. Alignment of these peptides yields a tentative structure for the entire fragment, which is in exact agreement with the amino acid composition deduced from acid hydrolysates. © 1969, American Chemical Society. All rights reserved.

引用

页码：3859 / +

页数：1

共 11 条

[1]

BARGETZI J, 1964, J BIOL CHEM, V239, P3767

[2]

BRADSHAW RA, 1969, J BIOL CHEM, V244, P2149

[3] AMINO ACID SEQUENCE OF BOVINE CARBOXYPEPTIDASE A .3. SPECIFICITY OF PEPTIDE-BOND CLEAVAGE BY THERMOLYSIN AND COMPLETE SEQUENCE OF CYANOGEN BROMIDE FRAGMENT F3 [J].