Pepsinogen C and pepsin C. Further purification and amino acid composition

Pepsinogen C and pepsin C from the pig have been further purified by chromatography on DEAE-cellulose and by exclusion chromatography and the specific activities (with haemoglobin substrate) found are higher than those previously reported. The final preparations are homogeneous on electrophoresis in...

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Bibliographic Details
Published inBiochemical journal Vol. 101; no. 1; pp. 176 - 183
Main Authors Ryle, A P, Hamilton, M P
Format Journal Article
LanguageEnglish
Published England 01.10.1966
Subjects
Amino Acids - analysis
Animals
Chromatography
Electrophoresis
Enzyme Precursors - analysis
In Vitro Techniques
Pepsin A - analysis
Swine
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Summary:Pepsinogen C and pepsin C from the pig have been further purified by chromatography on DEAE-cellulose and by exclusion chromatography and the specific activities (with haemoglobin substrate) found are higher than those previously reported. The final preparations are homogeneous on electrophoresis in starch gel at three pH values except for contamination with less than 4% of pepsinogen and pepsin respectively. Pepsinogen C, like pepsin C, contains no phosphate. The amino acid compositions show some marked differences from those of pepsinogen and pepsin especially in the content of basic amino acids, glutamic acid, aspartic acid, leucine and isoleucine. The molecular weights of the enzyme and zymogen, obtained from the amino acid compositions, are 41400 and 36000 respectively, similar to those of pepsinogen and pepsin.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Died January 1966.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj1010176