Agricultural and Biological Chemistry
Online ISSN : 1881-1280
Print ISSN : 0002-1369
ISSN-L : 0002-1369
Purification and Characterization of N-Acetylmuramyl-L-alanine Amidase from Streptomyces globisporus 1829
Shigeo KAWATATadashi TAKEMURAYoshiyuki TAKASEKanae YOKOGAWA
Author information
JOURNAL FREE ACCESS

1984 Volume 48 Issue 2 Pages 261-269

Details
Abstract
The enzyme, N-acetylmuramyl-L-alanine amidase (mucopeptide aminohydrolase EC 3.5. 1. 18) was found in mutanolysin, which was purified partially from the cultural broth of Streptomyces globisporus 1829. This enzyme was highly purified. The overall purification was 37.5-fold with a yield of 19.2% from mutanolysin. The molecular weight of the enzyme was 18, 500 as determined by plate gel filtration. The enzyme was inhibited by Cu++. This enzyme has a preference for substances of lower molecular weight and seems to be dependent on the prior action of a hexosamidase. This enzyme is not bacteriolytic per se.
Content from these authors

This article cannot obtain the latest cited-by information.

© Japan Society for Bioscience, Biotechnology, and Agrochemistry
Next article
feedback
Top