Physiological variant of antithrombin‐III lacks carbohydrate sidechain at Asn 135

  title={Physiological variant of antithrombin‐III lacks carbohydrate sidechain at Asn 135},
  author={Stephen O. Brennan and Peter M. George and Robert E. Jordan},
  journal={FEBS Letters},
Both normal antithrombin‐III (AT‐IIIα) and the high heparin affinity form (AT‐IIIβ) were isolated from pooled human plasma. AT‐IIIβ had a lower negative charge and lower molecular mass than AT‐IIIα. Sialidase and endo‐F digestion indicated that the inherent difference resided in the oligosaccharide component of the molecule. CNBr fragmentation showed there was an oligosaccharide sidechain missing between residues 104 and 251, subdigestion with trypsin indicated that Asn 135 was not glycosylated… Expand
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Interactions Between The Functional Domains of Antithrombin III
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Separation of antithrombin III variants by micellar electrokinetic chromatography.
Micellar electrokinetic chromatography was used to analytically separate these AT III variants, which differ in their affinity to the polysaccharide heparin. Expand
Antithrombin Glasgow, 393 arg to his: A P1 reactive site variant with increased heparin affinity but no thrombin inhibitory activity
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Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity.
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The molecular abnormality of albumin Parklands: 365 Asp----His.
  • S. Brennan
  • Biology, Medicine
  • Biochimica et biophysica acta
  • 1985
An electrophoretically slow albumin variant was isolated from the plasma of a patient with bisalbuminemia and confers on albumin Parklands a greater resistance to partial acid hydrolysis, a feature which, when employed together with SDS-gel electrophoresis, can be used as a diagnostic test for the presence of this variant. Expand
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