Literature DB >> 2049865

Characterization of human plasma sialytransferase using a novel fluorometric assay.

H J Gross1, R Brossmer.   

Abstract

We have characterized human plasma sialytransferase using a new fluorometric assay based on incorporation of a fluorescent NeuAc analogue into different acceptor glycoconjugates. This enables an exact characterization of acceptor specificity and kinetic properties. The data obtained indicate the presence of at least two distinct plasma sialytransferases: one specific for N-linked complex type glycan acceptors, and the other for GalNAc-residues on O-linked glycan acceptors. The first enzyme turned out to have very similar properties to a purified human liver sialytransferase, supporting an earlier hypothesis that liver is the main enzyme source. The new fluorometric assay presented here may be suitable for answering the question as to whether plasma sialytransferase is a useful diagnostic parameter in pathology.

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Year:  1991        PMID: 2049865     DOI: 10.1016/0009-8981(91)90144-2

Source DB:  PubMed          Journal:  Clin Chim Acta        ISSN: 0009-8981            Impact factor:   3.786


  4 in total

1.  Role of sialyltransferases involved in the biosynthesis of Lewis antigens in human pancreatic tumour cells.

Authors:  Rosa Peracaula; Glòria Tabarés; Anna López-Ferrer; Reinhard Brossmer; Carme de Bolós; Rafael de Llorens
Journal:  Glycoconj J       Date:  2005-03       Impact factor: 2.916

Review 2.  Polyacrylamide-based glycoconjugates as tools in glycobiology.

Authors:  N V Bovin
Journal:  Glycoconj J       Date:  1998-05       Impact factor: 2.916

Review 3.  Fluorescently labelled glycans and their applications.

Authors:  Hongbin Yan; Ravi Shekar Yalagala; Fengyang Yan
Journal:  Glycoconj J       Date:  2015-08-04       Impact factor: 2.916

Review 4.  Exploration of the Sialic Acid World.

Authors:  Roland Schauer; Johannis P Kamerling
Journal:  Adv Carbohydr Chem Biochem       Date:  2018-11-28       Impact factor: 12.200

  4 in total

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