Endo-beta-N-acetylglucosaminidases acting on carbohydrate moieties of glycoproteins: purification and properties of the two enzymes with different specificities from Clostridium perfringens.

Archives of biochemistry and biophysics ·Vol. 171 ·No. 1 ·1975-11-00 ·Pages 78-86

Ito S, Muramatsu T, Kobata A

Abstract

暂无摘要

MeSH Terms

Acetylglucosaminidase/isolation & purification,metabolism Cations, Divalent Chromatography, Gel Chromatography, Ion Exchange Clostridium perfringens/enzymology Edetic Acid/pharmacology Glycoproteins Hexosaminidases/metabolism Hydrogen-Ion Concentration Isoenzymes/isolation & purification,metabolism Kinetics Structure-Activity Relationship Sulfhydryl Reagents/pharmacology

Chemicals

Cations, Divalent Glycoproteins Isoenzymes Sulfhydryl Reagents Edetic Acid Hexosaminidases Acetylglucosaminidase

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Ito S

Muramatsu T

Kobata A

Article Info

Journal

Archives of biochemistry and biophysics

Abbr.

Arch Biochem Biophys

ISSN

0003-9861

DOI

10.1016/0003-9861(75)90009-0

Published

1975-11-00

Pages

78-86

Language

English

Region

United States

NLM ID

0372430

Subset

External Links

PubMed source DOI: 10.1016/0003-9861(75)90009-0 View journal details

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Endo-beta-N-acetylglucosaminidases acting on carbohydrate moieties of glycoproteins: purification and properties of the two enzymes with different specificities from Clostridium perfringens.

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