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Biodegradability of synthetic branched polypeptide with poly(L-lysine) backbone.
- Source :
-
Biological chemistry Hoppe-Seyler [Biol Chem Hoppe Seyler] 1989 Sep; Vol. 370 (9), pp. 1019-26. - Publication Year :
- 1989
-
Abstract
- A detailed investigation is reported about the biodegradation of poly[Lys(DL-Alam)], m approximately 3, (AK) the common inside area of a branched polypeptide model system developed by our group over the last decade. Enzymatic hydrolysis was carried out by the exopeptidase aminopeptidase M, or the endopeptidase trypsin, or their mixture. Ion-exchange column chromatography, paper electrophoresis and thin-layer chromatography were utilised to achieve separation of metabolites. Breakdown products were identified by the aid of synthetic oligopeptides representing the potential fragments (DL-Ala2, DL-Ala3, Lys(DL-Alam), m = 1-3). The kinetics and the degree of enzymatic degradation were determined. The ratio of peptide/amino acid amounts in the hydrolysate was found to be 1.07 after 24 h treatment with aminopeptidase M, 3.0 with trypsin and 1.3 with aminopeptidase - trypsin mixture. The overall results indicated that the proteolysis of AK by an aminopeptidase M and trypsin mixture proceeds stepwise at multiple sites on the polypeptide chain. The degradation is significantly retarded as compared to that of alpha- or epsilon-polylysine. A mechanism of degradation is suggested based on the experimental results.
- Subjects :
- Alanine metabolism
Amino Acid Sequence
Biodegradation, Environmental
CD13 Antigens
Chromatography, Ion Exchange
Chromatography, Thin Layer
Electrophoresis, Paper
Kinetics
Molecular Sequence Data
Peptide Fragments chemical synthesis
Peptide Fragments metabolism
Alanine analogs & derivatives
Aminopeptidases metabolism
Dipeptides metabolism
Oligopeptides metabolism
Polylysine metabolism
Trypsin metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0177-3593
- Volume :
- 370
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Biological chemistry Hoppe-Seyler
- Publication Type :
- Academic Journal
- Accession number :
- 2575393
- Full Text :
- https://doi.org/10.1515/bchm3.1989.370.2.1019