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Inhibition of aspartic proteinases by synthetic peptides derived from the propart region of human prorenin.
- Source :
-
The International journal of biochemistry [Int J Biochem] 1992 Feb; Vol. 24 (2), pp. 297-301. - Publication Year :
- 1992
-
Abstract
- 1. Five synthetic peptides which together spanned the propart segment of human prorenin were tested for their ability to interact with human renin, pepsin, gastricsin, cathepsin D, cathepsin E, calf chymosin and the aspartic proteinase from Endothia parasitica. 2. While two peptides showed no significant effect with any of the enzymes, a further two were cleaved by several enzymes. 3. Only one (corresponding to the 32P-43P residues in the propart sequence) acted as a weak competitive inhibitor of most of the enzymes.
- Subjects :
- Amino Acid Sequence
Amino Acids analysis
Animals
Cattle
Enzyme Precursors chemistry
Humans
Molecular Sequence Data
Peptides chemical synthesis
Peptides chemistry
Peptides pharmacology
Renin chemistry
Aspartic Acid Endopeptidases antagonists & inhibitors
Enzyme Precursors physiology
Renin physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0020-711X
- Volume :
- 24
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- The International journal of biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 1733796
- Full Text :
- https://doi.org/10.1016/0020-711x(92)90261-x