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Updated: Oct 9, 2026

Improving IV Insulin Administration in a Community Hospital
Published on: June 11, 2012
Covalent glycoinositolphospholipid binding to hemoglobin: a new post-translational modification of Hb occurring in
V Niketić1, N Tomasević, M Nikolić
1Department of Chemistry, University of Belgrade, Yugoslavia. vniketic@chem.bg.ac.yu
Abstract:
In this work a novel hitherto unrecognised minor hemoglobin (Hb) fraction, which we detected previously in hemolysates of erythrocytes exposed to a high concentration of insulin under hypoglycemic conditions, both in vivo and in vitro, is analysed. The modification of Hb in HbA1x was shown to be due the addition of glycoinositolphospholipid (GPI) to the C termini of both beta polypeptide chains. A structurally related minor Hb fraction was identified in erythrocytes exposed in vitro to insulin-mimetic agent, trypsin. To our knowledge this is the first demonstration of such a modification of Hb, as well as the first demonstration of post-translational GPI binding to proteins in response to insulin. The mechanism proposed for GPI-Hb formation is briefly described.
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