Purification of human liver glycoprotein sialyltransferase by affinity chromatography.
作者信息
Alhadeff J A, Holzinger R T
出版信息
J Biochem Biophys Methods. 1982 Aug;6(3):229-33. doi: 10.1016/0165-022x(82)90045-8.
PMID:7130620
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.
摘要
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