The Amino Acid Sequences of Some Tryptic Peptides from Porcine Pepsinogen

Pepsinogen was reduced, carboxymethylated, and hydrolyzed with trypsin. The resulting mixture of peptides was fractionated ( a ) on a column of Sephadex G-25, ( b ) on Amberlite IR-120-A2 followed by high voltage electrophoresis, and ( c ) by peptide mapping. Eight peptides, varying in length from t...

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Bibliographic Details
Published in:The Journal of biological chemistry 1968-12, Vol.243 (23), p.6099-6103
Main Authors: Koehn, P V, Perlmann, G E
Format: Article
Language:English
Subjects:
Alanine - analysis
Amino Acid Sequence
Animals
Arginine - analysis
Asparagine - analysis
Chromatography, Gel
Chromatography, Ion Exchange
Electrophoresis
Enzyme Precursors - analysis
Glycine - analysis
Histidine - analysis
Leucine - analysis
Lysine - analysis
Pepsin A
Peptides - analysis
Proline - analysis
Swine
Trypsin
Valine - analysis
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Summary:Pepsinogen was reduced, carboxymethylated, and hydrolyzed with trypsin. The resulting mixture of peptides was fractionated ( a ) on a column of Sephadex G-25, ( b ) on Amberlite IR-120-A2 followed by high voltage electrophoresis, and ( c ) by peptide mapping. Eight peptides, varying in length from two to eight amino acids were isolated and their amino acid sequences were determined. Six of these peptides and free lysine could be assigned to the NH 2 -terminal portion of pepsinogen which is released on activation. The amino acid composition of these peptides accounts for 32 of the 41 residues liberated, including 7 of the 9 lysines, 1 histidine, and 2 arginines. Two additional peptides (I) Ala-Asn-Asn-Lys and (II) Val-Gly-Leu-Ala-Pro-Val-Ala were characterized and assigned to the COOH-terminal part of pepsinogen, with alanine of Peptide II being the COOH terminus.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)94465-0