N-terminal sequence of swine pepsinogen and pepsin. The site of pepsinogen activation

The sequence of 119 amino acids of swine pepsinogen comprising the fragment released during the zymogen activation as well as the N-terminal part of pepsin is established. The activation of swine pepsinogen is shown to be accompanied by specific cleavage of Leu-Ile bond in the sequence: Ala 41 Ala A...

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Published inBiochemical and biophysical research communications Vol. 54; no. 3; pp. 1164 - 1170
Main Authors Stepanov, V.M., Baratova, L.A., Pugacheva, I.B., Belyanova, L.P., Revina, L.P., Timokhina, E.A.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.10.1973
Subjects
Amino Acid Sequence
Animals
Aspartic Acid
Chromatography, DEAE-Cellulose
Enzyme Activation
Hydrolysis
Isoleucine - analysis
Leucine - analysis
Pepsin A - metabolism
Pepsinogens - metabolism
Peptide Chain Termination, Translational
Swine
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Summary:The sequence of 119 amino acids of swine pepsinogen comprising the fragment released during the zymogen activation as well as the N-terminal part of pepsin is established. The activation of swine pepsinogen is shown to be accompanied by specific cleavage of Leu-Ile bond in the sequence: Ala 41 Ala Ala Leu Ile Gly 46 where Ile-45 represents the N-terminal residue of pepsin. This sequence is attacked in the course of pepsinogen activation by external enzymes — neutral proteinases and elastase.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(73)90814-0