Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Bacteriolytic enzymes from the blood plasma of the sheep

Bacteriolytic enzymes from the blood plasma of the sheep Bacteriolytic factors from the blood plasma of healthy sheep have been studied. Three enzymes not described earlier in the literature have been identified and characterized. Two enzymes exhibit activity toward Escherichia coli and have molecular weights of 15 ± 2 kDa. The third enzyme that exhibits activity toward E. coli and Micrococcus luteus has a molecular weight of 34 ± 4 kDa. The kinetic parameters of bacterial lysis for all enzymes have been determined; in particular, optimal pH values for each of the substrates used have been found. For the identification of the enzymes, trypsinolysis and a mass-spectroscopic study of fragments have been carried out. The results were compared with the data on sheep proteins available in the Swiss-Prot, NCBI, and MSDB databases. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Bioorganic Chemistry Springer Journals

Loading next page...
 
/lp/springer-journals/bacteriolytic-enzymes-from-the-blood-plasma-of-the-sheep-0yZ7BSjAFD

References (2)

Publisher
Springer Journals
Copyright
Copyright © 2012 by Pleiades Publishing, Ltd.
Subject
Life Sciences; Biomedicine general; Bioorganic Chemistry; Organic Chemistry; Biochemistry, general
ISSN
1068-1620
eISSN
1608-330X
DOI
10.1134/S1068162012030132
Publisher site
See Article on Publisher Site

Abstract

Bacteriolytic factors from the blood plasma of healthy sheep have been studied. Three enzymes not described earlier in the literature have been identified and characterized. Two enzymes exhibit activity toward Escherichia coli and have molecular weights of 15 ± 2 kDa. The third enzyme that exhibits activity toward E. coli and Micrococcus luteus has a molecular weight of 34 ± 4 kDa. The kinetic parameters of bacterial lysis for all enzymes have been determined; in particular, optimal pH values for each of the substrates used have been found. For the identification of the enzymes, trypsinolysis and a mass-spectroscopic study of fragments have been carried out. The results were compared with the data on sheep proteins available in the Swiss-Prot, NCBI, and MSDB databases.

Journal

Russian Journal of Bioorganic ChemistrySpringer Journals

Published: May 23, 2012

There are no references for this article.