ArticleGlycoconjugate journal2008
Isolation and properties of two sialate-O-acetylesterases from horse liver with 4- and 9-O-acetyl specificities.
Article in Glycoconjugate journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Modified Sialic Acids on Mucus and Erythrocytes Inhibit Influenza A Virus Hemagglutinin and Neuraminidase Functions.Journal of virology · 2020Article
- Review
- Review
- Exploration of the Sialic Acid World.Advances in carbohydrate chemistry and biochemistry · 2018Review
- A Chemical Biology Solution to Problems with Studying Biologically Important but Unstable 9-O-Acetyl Sialic Acids.ACS chemical biology · 2017Article
- Advanced Technologies in Sialic Acid and Sialoglycoconjugate Analysis.Topics in current chemistry · 2015Review
- Functions and Biosynthesis of O-Acetylated Sialic Acids.Topics in current chemistry · 2015Review
- Sialic acids siglec interaction: a unique strategy to circumvent innate immune response by pathogens.The Indian journal of medical research · 2013Review
- Modifications of glycans: biological significance and therapeutic opportunities.ACS chemical biology · 2012Review
- O-Acetylated sialic acids and their role in immune defense.Advances in experimental medicine and biology · 2011Article
- Assays of sialate-O-acetyltransferases and sialate-O-acetylesterases.Glycoconjugate journal · 2009Article
- Sialic acids as regulators of molecular and cellular interactions.Current opinion in structural biology · 2009Review
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sialate-O-acetylesterase was purified almost 900-fold from particle-free supernatants of horse liver by gel filtration, ion-exchange chromatography and isoelectric focussing. The native enzyme on gel filtration exhibits a molecular weight of 54,000 Da. It was separated by isoelectric focussing into two forms with pI values of 4.8 and 5.7, respectively. The esterase with a lower pI hydrolyses only 9-O-acetyl groups from sialic acids (K(M) 1.1 mM), while that with the higher pI esterifies both 4- and 9-O-acetylated monosaccharides at similar rates (K(M) 0.3 M and 1.3 mM, respectively). Both forms are inactive with 7-O-acetylated N-acetylneuraminic acid. Enzyme assays were carried out at the pH optimum (pH 8.4-8.6) using free O-acetylated sialic acids followed by direct analysis of the reaction products by isocratic anion-exchange HPLC. Glycosidically bound sialic acids can also be de-O-acetylated. Horse liver esterase seems to be an essential enzyme for the catabolism of 4-O-acetylated sialoglycoconjugates, since sialidase from this tissue cannot act on 4-O-acetylated sialic acids.
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