Document Detail


Characterisation of the enzymatic 4-O-acetylation of sialic acids in microsomes from equine submandibular glands.
MedLine Citation:
PMID:  11511809     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Microsomes prepared from equine submandibular glands and incubated with tritium-labelled AcCoA incorporated acid-insoluble radioactivity in a manner dependent on time, protein, membrane integrity and AcCoA concentration, with incorporation being optimal at 37 degrees C and pH 6.6. Under the experimental conditions used a K(M) of 32.1 microM for AcCoA and a V(max) of 1.2 pmol/mg protein x min was obtained. The incorporation of acid-insoluble radioactivity was also inhibited by CoA in a competitive manner (K(i)=240 microM), as well as by para-chloromercuribenzoate, 3'-dephospho-CoA, 5'-IDP, 5'-ADP, beta-NAD and 4,4'-diisothiocyanatostilbene-2,2'-disulfonate. We demonstrate here that this incorporation of radioactivity into endogenous sialic acid is due to the action of an AcCoA:sialate-4-O-acetyltransferase [EC 2.3.1.44]. Radio thin-layer chromatography analyses of propionic acid-released sialic acids showed that the incorporation of radioactivity correlated with the formation of a radiolabelled species that co-migrated with authentic Neu4,5Ac2. Saponification experiments using NaOH, mouse hepatitis virus strain S and Influenza C/JJ/50 virus also showed that the transfer of [3H]acetyl groups from [3H]AcCoA to endogenous sialic acid acceptors was occurring exclusively at carbon 4 of the pyranose ring.
Authors:
J Tiralongo; H Schmid; R Thun; M Iwersen; R Schauer
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Glycoconjugate journal     Volume:  17     ISSN:  0282-0080     ISO Abbreviation:  Glycoconj. J.     Publication Date:  2000 Dec 
Date Detail:
Created Date:  2001-08-20     Completed Date:  2002-01-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8603310     Medline TA:  Glycoconj J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  849-58     Citation Subset:  IM    
Affiliation:
Biochemisches Institut, Christian-Albrechts-Universität, Olshausenstr. 40, D-24098 Kiel, Germany.
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MeSH Terms
Descriptor/Qualifier:
Acetyl Coenzyme A / metabolism
Acetylation
Animals
Cattle
Chromatography, High Pressure Liquid
Chromatography, Thin Layer
Fluorescence
Horses*
Hydrogen-Ion Concentration
Kinetics
Microsomes / chemistry,  enzymology,  metabolism
Radiography
Sialic Acids / analysis,  metabolism*
Submandibular Gland / chemistry,  enzymology,  metabolism*
Temperature
Chemical
Reg. No./Substance:
0/Sialic Acids; 72-89-9/Acetyl Coenzyme A

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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