Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by MORITA, T.
Right arrow Articles by MATSUSHIMA, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by MORITA, T.
Right arrow Articles by MATSUSHIMA, Y.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1978, Vol. 83, No. 3 893-903
© 1978 Japanese Biochemical Society

research-article

Purification and Characterization of Lysozyme Produced by Streptomyces erythraeus

Takashi MORITA, Saburo HARA and Yoshio MATSUSHIMA

Department of Chemistry, College of Science, Osaka University Toyonaka, Osaka 560

A species of lysozyme (SE lysozyme) was purified from culture filtrate of Streptomyces erythraeus. The enzyme has a molecular weight of 18,500 as determined by ultracentrifugation. Its isoelectric point is 9.5, and it shows optimal activity at pH 4.0 with an optimal ionic strength of 0.1. Investigation of the substrate specificity showed SE lysozyme to be an N-acetyl-muramidase. The simplest product in the digest of cell walls of Micrococcus lysodeikticus was identified as a disaccharide, [GlcNAcß(1{uparrow}4)MurNAc]. While S. aureus as well as M. lysodeikticus was lysed by this lysozyme, chitin and its derivatives were not.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
A. Rau, T. Hogg, R. Marquardt, and R. Hilgenfeld
A New Lysozyme Fold. CRYSTAL STRUCTURE OF THE MURAMIDASE FROM STREPTOMYCES COELICOLOR AT 1.65 A RESOLUTION
J. Biol. Chem., August 17, 2001; 276(34): 31994 - 31999.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.