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Microbial degradation of physiologically active peptides by strain B-9.
- Source :
- Analytical & Bioanalytical Chemistry; Oct2012, Vol. 403 Issue 7, p1783-1791, 9p
- Publication Year :
- 2012
-
Abstract
- The reaction of some physiologically active peptides with bacterial strain B-9 has been investigated. Bradykinin, β-endorphin, and [Leu]enkephalin were quickly degraded, with half-lives of <5 min. Somatostatin, substance P, and angiotensin I were degraded relatively smoothly, with half-lives of 10 min to 1 h, whereas oxytocin and insulin were slowly degraded, with half-lives of 1 and 4 days, respectively. Vasopressin was barely degraded, with a half-life of >7 days. Linearized vasopressin, prepared by the reductive cleavage of the disulfide bond followed by alkylation with iodoacetamide, was degraded significantly faster than intact vasopressin, with a half-life of 2.5 h. A loop formed by disulfide bond formation was regarded as one of the degradation-resistant factors. Hydrolysis of the peptides in this study took place through cleavage of various peptide bonds, and the strain B-9 may bear similarities to the neutral endopeptidase in terms of its broad selectivity. [ABSTRACT FROM AUTHOR]
- Subjects :
- PEPTIDES
ORGANIC compounds
BRADYKININ
KININS
NEUROPEPTIDES
Subjects
Details
- Language :
- English
- ISSN :
- 16182642
- Volume :
- 403
- Issue :
- 7
- Database :
- Complementary Index
- Journal :
- Analytical & Bioanalytical Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 75447952
- Full Text :
- https://doi.org/10.1007/s00216-011-5635-6