JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Takagaki, K.
Right arrow Articles by Endo, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Takagaki, K.
Right arrow Articles by Endo, M.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 265, Issue 2, 854-860, Jan, 1990

Isolation and characterization of Patnopecten mid-gut gland endo-beta- xylosidase active on peptidochondroitin sulfate

K Takagaki, A Kon, H Kawasaki, T Nakamura, S Tamura and M Endo
Department of Biochemistry, Hirosaki University School of Medicine, Japan.

An endo-beta-xylosidase acting on the linkage region of peptidochondroitin sulfate was isolated from the mid-gut gland of the mollusc Patnopecten and purified about 375-fold, using a combination of ammonium sulfate fractionation, gel filtration on Sephacryl S-200, and DEAE-Sephacel chromatography. The pH optimum and the isoelectric point of this enzyme were 4.0 and 7.0, respectively. The molecular weight, estimated by gel filtration through Sephacryl S-200, was 78,000. The purified enzyme was completely free from protease, exoglycosidases, sulfatase, and phosphatase. This enzyme hydrolyzed the xylosyl serine linkage of the linkage region of various glycosaminoglycans, that is chondroitin sulfate, dermatan sulfate and heparan sulfate, all possessing a very small peptide segment, but not proteoglycans. It was concluded that this endo-beta-xylosidase was involved in the catabolism of proteoglycans.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
K. Takagaki, M. Iwafune, I. Kakizaki, K. Ishido, Y. Kato, and M. Endo
Cleavage of the Xylosyl Serine Linkage between a Core Peptide and a Glycosaminoglycan Chain by Cellulases
J. Biol. Chem., May 17, 2002; 277(21): 18397 - 18403.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Ishido, K. Takagaki, M. Iwafune, S. Yoshihara, M. Sasaki, and M. Endo
Enzymatic Attachment of Glycosaminoglycan Chain to Peptide Using the Sugar Chain Transfer Reaction with Endo-beta -xylosidase
J. Biol. Chem., March 29, 2002; 277(14): 11889 - 11895.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Saitoh, K. Takagaki, M. Majima, T. Nakamura, A. Matsuki, M. Kasai, H. Narita, and M. Endo
Enzymic Reconstruction of Glycosaminoglycan Oligosaccharide Chains Using the Transglycosylation Reaction of Bovine Testicular Hyaluronidase
J. Biol. Chem., February 24, 1995; 270(8): 3741 - 3747.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1990 by the American Society for Biochemistry and Molecular Biology.