Journal ArticleOPEN ACCESS

Enzymatic Properties of an Extracellular Phospholipase C Purified from a Marine Streptomycete

Bioscience, Biotechnology and Biochemistry (2009) 73(9) 2136-2137
DOI: 10.1271/bbb.90323
22Citations
Citations of this article
9Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

A novel extracellular phospholipase C (PLC) was purified from a marine streptomycete. It had a molecular mass of 28 kDa as estimated by SDS-polyacrylamide gel electrophoresis. Its enzyme activity was optimal at pH 8.0 at 45 °C. The PLC hydrolyzed only phosphatidylcholine. Its activity was enhanced 300% by Na+ (200 mM), suggesting that the purified PLC is a typical marine-type enzyme.

Author supplied keywords

Cite

CITATION STYLE

APA

Mo, S., Kim, J. H., & Cho, K. W. (2009). Enzymatic Properties of an Extracellular Phospholipase C Purified from a Marine Streptomycete. Bioscience, Biotechnology and Biochemistry, 73(9), 2136–2137. https://doi.org/10.1271/bbb.90323

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free