Purification of human liver glycoprotein sialyltransferase by affinity chromatography.
Publication/Presentation Date
8-1-1982
Abstract
A simple procedure has been developed for purifying solubilized human liver glycoprotein sialyltransferase (EC 2.4.99.1) 16000-fold in 4-5% yield. The procedure involves two centrifugation steps, affinity chromatography of the ultrasupernatant fluid on cytidine diphosphate-hexanolamine-agarose followed by gel filtration on Sephadex G-150. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) indicated that the purified sialyltransferase preparation contains approximately equivalent amounts of three protein bands (with apparent molecular weights of 61000, 63000 and 70000) and is highly purified if not homogeneous.
Volume
6
Issue
3
First Page
229
Last Page
233
ISSN
0165-022X
Published In/Presented At
Alhadeff, J. A., & Holzinger, R. T. (1982). Purification of human liver glycoprotein sialyltransferase by affinity chromatography. Journal of biochemical and biophysical methods, 6(3), 229–233. https://doi.org/10.1016/0165-022x(82)90045-8
Disciplines
Medicine and Health Sciences
PubMedID
7130620
Department(s)
Department of Medicine
Document Type
Article