Purification of α 2,6-sialyltransferase from rat liver by dye chromatography
- 15 July 1988
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 253 (2) , 577-580
- https://doi.org/10.1042/bj2530577
Abstract
We describe a simple three-step purification for Gal-beta 1,4-GlcNAc-alpha 2,6-sialyltransferase (EC 2.4.99.1) from rat liver which uses chromatography on Cibacron Blue F3GA and f.p.l.c. It gives a highly purified (11,000-fold) enzyme in 19% yield, which is free of other sialyltransferases, CMP-NeuAc hydrolase, sialidases and proteinases.This publication has 15 references indexed in Scilit:
- Activation and transfer of novel synthetic 9‐substituted sialic acidsEuropean Journal of Biochemistry, 1987
- Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymesAnalytical Biochemistry, 1984
- Purification of human liver glycoprotein sialyltransferase by affinity chromatographyJournal of Biochemical and Biophysical Methods, 1982
- Protein purification using immobilised triazine dyesJournal of Chromatography A, 1979
- Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-α-d-N-acetylneuraminate) substrateAnalytical Biochemistry, 1979
- Comparative Aspects of Glycoprotein StructureAnnual Review of Biochemistry, 1976
- The Role of Surface Carbohydrates in the Hepatic Recognition and Transport of Circulating GlycoproteinsPublished by Wiley ,1974
- Methyl-14C-glycinated hemoglobin as a substrate for proteasesBiochimica et Biophysica Acta (BBA) - Enzymology, 1971
- Simulation of water movement across the cell membrane in a hypertonic mediumComputers in Biology and Medicine, 1970
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970