Abstract
The presence in the 100,000 g supernatant of rat brain homogenate of an inhibitor of the sialyltransferase has been confirmed. It is also present in chicken and bovine brain and in other rat and bovine organs. The inhibitor has been purified, a preparation with a specific activity 130-fold higher than that of the original 100,000 g supernatant of brain being obtained. It runs as a single peak in polyacrylamide-gel electrophoresis; when run in the presence of SDS, two components appeared. The apparent Mr of the components were 14,800 and 22,400. The inhibitor has been characterized as a heat-stable protein of acidic nature. It has effect on the glycolipid and the glycoprotein sialyltransferase activities but has no effect on the galactosaminyltransferase activity.
MeSH Terms
Amino Acids/analysis
Animals
Asialoglycoproteins
Brain/enzymology
Cattle
Chickens
Chromatography, Gel
Chromatography, Ion Exchange
Chymotrypsin/pharmacology
Fetuins
Kinetics
Molecular Weight
Rats
Sialyltransferases/antagonists & inhibitors
Species Specificity
Temperature
Tissue Distribution
Trypsin/pharmacology
alpha-Fetoproteins/pharmacology
Chemicals
Amino Acids
Asialoglycoproteins
Fetuins
alpha-Fetoproteins
asialofetuin
Sialyltransferases
beta-D-galactoside alpha 2-6-sialyltransferase
Chymotrypsin
Trypsin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Albarracin I
Departamento de Química Biológica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Argentina.
Lassaga F E
Caputto R
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