Literature DB >> 7130620

Purification of human liver glycoprotein sialyltransferase by affinity chromatography.

J A Alhadeff, R T Holzinger.   

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.

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Year:  1982        PMID: 7130620     DOI: 10.1016/0165-022x(82)90045-8

Source DB:  PubMed          Journal:  J Biochem Biophys Methods        ISSN: 0165-022X


  3 in total

1.  Purification of alpha 2,6-sialyltransferase from rat liver by dye chromatography.

Authors:  U Sticher; H J Gross; R Brossmer
Journal:  Biochem J       Date:  1988-07-15       Impact factor: 3.857

2.  Purification and characterization of alpha (2-6)-sialyltransferase from human liver.

Authors:  U Sticher; H J Gross; R Brossmer
Journal:  Glycoconj J       Date:  1991-02       Impact factor: 2.916

Review 3.  Increasing the α 2, 6 sialylation of glycoproteins may contribute to metastatic spread and therapeutic resistance in colorectal cancer.

Authors:  Jung-Jin Park; Minyoung Lee
Journal:  Gut Liver       Date:  2013-11-11       Impact factor: 4.519

  3 in total

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