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PMID: 4509655 Published · ppublish English Journal Article

Qualitative differences in the N-acetyl-D-galactosaminyltransferases produced by human A1 and A2 genes.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 70 ·No. 1 ·1973-01-00 ·Pages 220-4

Schachter H, Michaels MA, Tilley CA, Crookston MC, Crookston JH

Abstract

This study describes the kinetic properties of N-acetyl-D-galactosaminyltransferase in serum from subjects with blood groups A(1) and A(2). When the A(1) and A(2) enzymes were compared, with lacto-N-fucopentaose I and 2'-fucosyllactose as acceptors, the enzymes differed in their cation requirements, pH optima, and K(m) values. The two acceptors competed for the same transferase. Mixing experiments showed that the lower activity of the A(2) enzyme could not be attributed to a modifier or inhibitor in serum. It was concluded that the A(1) and A(2) enzymes differ qualitatively.

MeSH Terms
ABO Blood-Group System Buffers Carbon Isotopes Catalysis Chromatography Galactosamine Genes Genotype Humans Hydrogen-Ion Concentration Ions Kinetics Magnesium/metabolism Manganese/metabolism Oligosaccharides/analysis,metabolism Transferases/biosynthesis,blood,metabolism
Chemicals
ABO Blood-Group System Buffers Carbon Isotopes Ions Oligosaccharides Manganese Galactosamine Transferases Magnesium
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Schachter H
Michaels M A
Tilley C A
Crookston M C
Crookston J H
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25 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.70.1.220
Published
1973-01-00
Pages
220-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC433219
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.70.1.220 PMC Full Text View journal details
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