SEPARATION OF PORCINE PEPSINOGEN-A AND PROGASTRICSIN - SEQUENCING OF THE 1ST 73 AMINO-ACID-RESIDUES IN PROGASTRICSIN

被引：17

作者：

FOLTMANN, B ^{[1
]}

DROHSE, HB ^{[1
]}

NIELSEN, PK ^{[1
]}

JAMES, MNG ^{[1
]}

机构：

[1] UNIV ALBERTA,DEPT BIOCHEM,MED RES COUNCIL CANADA,PROT STRUCT & FUNCT GRP,EDMONTON T6G 2E1,ALBERTA,CANADA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1121卷 / 1-2期

关键词：

ZYMOGEN; ASPARTIC PROTEINASE; ACTIVATION; PROSEGMENT PEPTIDE; SEQUENCE HOMOLOGY;

D O I：

10.1016/0167-4838(92)90339-F

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：

Porcine pepsinogen A (EC 3.4.23.1) and progastricsin (EC 3.4.23.3) have been separated by chromatography on DEAE-cellulose followed by chromatography on DEAE-Sepharose. Agar gel electrophoresis at pH 6.0 showed thc presence of three components of pepsinogen A and two of progastricsin. During activation at pH 2 a segment of 43 amino acid residues (the prosegment peptide) is cleaved from the N-terminus of progastricsin. The sequence of this was determined; in addition, the first 30 residues of gastricsin were sequenced. The sequence of the first 73 amino acid residues of progastricsin shows an overall identity with progastricsins from man, monkey and rat of 67%. The overall identity with other zymogens for gastric proteinases is 27%. The highly conserved Lys36p (pig pepsinogen A numbering) is changed to Arg in porcine progastricsin.

引用

页码：75 / 82

页数：8

共 28 条

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