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Amino-Acid Sequence of the Peptide Segment Liberated during Activation of Prochymosin (Prorennin).
- Source :
- European Journal of Biochemistry; Jun75 Part 2, Vol. 55 Issue 1, p95-103, 9p
- Publication Year :
- 1975
-
Abstract
- By conversion of prochymosin into active chymosin an N-terminal segment of 42 amino acid residues is liberated. In one activation experiment this segment was recovered in two peptides; in a second experiment the activation segment was cleaved into three peptides. The primary structures of the peptides have been determined. Overlaps between these peptides and between the activation segment and the active enzyme have been obtained from peptides produced by tryptic digestion of denatured prochymosin. Comparison of the amino acid sequences of the activation segments from bovine prochymosin, bovine pepsinogen and porcine pepsinogen shows considerable homology. [ABSTRACT FROM AUTHOR]
- Subjects :
- AMINO acids
PEPTIDES
ENZYMES
PEPSINOGEN
GASTRIC juice
HOMOLOGY (Biology)
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 55
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 15832477
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1975.tb02141.x