In this work a novel hitherto unrecognised hemoglobin (Hb) fraction, HbA1x, which we detected previously in hemolysates of erythrocytes exposed to high concentration of insulin under hypoglycemic conditions, both in vivo and in vitro, was analysed. Both β chains of Hb in HbA1x were found to be modified by covalent binding of a substance containing sugar, phosphate and fatty acid residues. HbA1x was therefore termed glycophospholipid (GPL) adduct (Hb-GPL). To our knowledge, this is the first demonstration of such modification of Hb, as well as the first demonstration of post-translational GPL binding to proteins in response to insulin binding to a cell. The mechanism proposed for Hb-GPL formation is briefly described.
Keywords:
Glycophospholipid / Hemoglobin / Insulin
Source:
Journal of the Serbian Chemical Society, 1996, 61, 7, 535-538
TY - JOUR
AU - Niketić, Vesna
AU - Tomašević, N
AU - Vajs, Vlatka
AU - Bojić, Ž
PY - 1996
UR - https://cer.ihtm.bg.ac.rs/handle/123456789/2794
AB - In this work a novel hitherto unrecognised hemoglobin (Hb) fraction, HbA1x, which we detected previously in hemolysates of erythrocytes exposed to high concentration of insulin under hypoglycemic conditions, both in vivo and in vitro, was analysed. Both β chains of Hb in HbA1x were found to be modified by covalent binding of a substance containing sugar, phosphate and fatty acid residues. HbA1x was therefore termed glycophospholipid (GPL) adduct (Hb-GPL). To our knowledge, this is the first demonstration of such modification of Hb, as well as the first demonstration of post-translational GPL binding to proteins in response to insulin binding to a cell. The mechanism proposed for Hb-GPL formation is briefly described.
PB - Serbian Chemical Society
T2 - Journal of the Serbian Chemical Society
T1 - Covalent glycophospholipid binding to hemoglobin. A new post-translational modification occurring in erythrocytes exposed to insulin
VL - 61
IS - 7
SP - 535
EP - 538
UR - https://hdl.handle.net/21.15107/rcub_cer_2794
ER -
@article{
author = "Niketić, Vesna and Tomašević, N and Vajs, Vlatka and Bojić, Ž",
year = "1996",
abstract = "In this work a novel hitherto unrecognised hemoglobin (Hb) fraction, HbA1x, which we detected previously in hemolysates of erythrocytes exposed to high concentration of insulin under hypoglycemic conditions, both in vivo and in vitro, was analysed. Both β chains of Hb in HbA1x were found to be modified by covalent binding of a substance containing sugar, phosphate and fatty acid residues. HbA1x was therefore termed glycophospholipid (GPL) adduct (Hb-GPL). To our knowledge, this is the first demonstration of such modification of Hb, as well as the first demonstration of post-translational GPL binding to proteins in response to insulin binding to a cell. The mechanism proposed for Hb-GPL formation is briefly described.",
publisher = "Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Covalent glycophospholipid binding to hemoglobin. A new post-translational modification occurring in erythrocytes exposed to insulin",
volume = "61",
number = "7",
pages = "535-538",
url = "https://hdl.handle.net/21.15107/rcub_cer_2794"
}
Niketić, V., Tomašević, N., Vajs, V.,& Bojić, Ž.. (1996). Covalent glycophospholipid binding to hemoglobin. A new post-translational modification occurring in erythrocytes exposed to insulin. in Journal of the Serbian Chemical Society
Serbian Chemical Society., 61(7), 535-538.
https://hdl.handle.net/21.15107/rcub_cer_2794
Niketić V, Tomašević N, Vajs V, Bojić Ž. Covalent glycophospholipid binding to hemoglobin. A new post-translational modification occurring in erythrocytes exposed to insulin. in Journal of the Serbian Chemical Society. 1996;61(7):535-538.
https://hdl.handle.net/21.15107/rcub_cer_2794 .
Niketić, Vesna, Tomašević, N, Vajs, Vlatka, Bojić, Ž, "Covalent glycophospholipid binding to hemoglobin. A new post-translational modification occurring in erythrocytes exposed to insulin" in Journal of the Serbian Chemical Society, 61, no. 7 (1996):535-538,
https://hdl.handle.net/21.15107/rcub_cer_2794 .
