A disulfide-bonded dimer of the golgi β-galactoside α2,6-sialyltransferase is catalytically inactive yet still retains the ability to bind galactose

Journal of Biological Chemistry

Volumn 271, Issue 13, 1996, Pages 7758-7766

  Ma, Jiyan ^a   Colley, Karen J ^a  

^a UNIVERSITY OF ILLINOIS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BOVINAE; ANIMALIA; BOS TAURUS;

AGAROSE; BETA GALACTOSIDE; CYTIDINE DIPHOSPHATE; DIMER; GALACTOSE; HEXANOL; IODOACETAMIDE; SIALYLTRANSFERASE;

ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CATALYSIS; CATTLE; DISULFIDE BOND; ENZYME DEGRADATION; GOLGI COMPLEX; LIVER; MALE; NONHUMAN; PRIORITY JOURNAL; RAT; REDUCTION;

ANIMALS; BINDING SITES; CATTLE; CENTRIFUGATION, DENSITY GRADIENT; CHROMATOGRAPHY, AFFINITY; DISULFIDES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPLASMIC RETICULUM, ROUGH; ENDOPLASMIC RETICULUM, SMOOTH; GALACTOSE; GOLGI APPARATUS; KINETICS; LIVER; MACROMOLECULAR SUBSTANCES; MOLECULAR WEIGHT; PEPTIDE MAPPING; RATS; SERINE ENDOPEPTIDASES; SIALYLTRANSFERASES;

EID: 0029871352     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.13.7758     Document Type: Article

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