Erythrocyte alterations in hemoglobin H disease

J. Szelényi, G. Lelkes, M. Horányi, J. Földi, I. Szász, S. Hollán

Research output: Article

3 Citations (Scopus)

Abstract

This study on erythrocytes in hemoglobin H (Hb-H) disease reveals that unstable Hb-H is bound to membranes to a greater extent, especially when it forms methemoglobin or is precipitated as an inclusion body. The methemoglobin content of these erythrocytes is elevated in spite of a higher activity of NADH-methemoglobin reductase. The ATPase activity is doubled and ATP is presumably used for phosphorylation of membrane proteins, which leads to cross-linking of membrane proteins. This assumption could be supported by the observed decrease in non-electrolyte permeability, by increased binding of hemoglobin to the membrane, and polymerisation of membrane proteins detected by SDS-polyacrylamide gel electrophoresis. By means of electron microscopy, it could also be shown that the inclusion bodies are bound to the inner surface of membrane and cause its protrusion. This linkage might be responsible for the observed inhibition of the lateral movement of intramembrane particles.

Original languageEnglish
Pages (from-to)961-967
Number of pages7
JournalActa Biologica et Medica Germanica
Volume40
Issue number7-8
Publication statusPublished - 1981

Fingerprint

alpha-Thalassemia
Methemoglobin
Membrane Proteins
Erythrocytes
Inclusion Bodies
Membranes
Hemoglobin H
Cytochrome-B(5) Reductase
Polymerization
Adenosine Triphosphatases
Polyacrylamide Gel Electrophoresis
Permeability
Electron Microscopy
Hemoglobins
Adenosine Triphosphate
Phosphorylation

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Erythrocyte alterations in hemoglobin H disease. / Szelényi, J.; Lelkes, G.; Horányi, M.; Földi, J.; Szász, I.; Hollán, S.

In: Acta Biologica et Medica Germanica, Vol. 40, No. 7-8, 1981, p. 961-967.

Research output: Article

Szelényi, J. ; Lelkes, G. ; Horányi, M. ; Földi, J. ; Szász, I. ; Hollán, S. / Erythrocyte alterations in hemoglobin H disease. In: Acta Biologica et Medica Germanica. 1981 ; Vol. 40, No. 7-8. pp. 961-967.
@article{37a2a7ed0402450e85d85d793de583c7,
title = "Erythrocyte alterations in hemoglobin H disease",
abstract = "This study on erythrocytes in hemoglobin H (Hb-H) disease reveals that unstable Hb-H is bound to membranes to a greater extent, especially when it forms methemoglobin or is precipitated as an inclusion body. The methemoglobin content of these erythrocytes is elevated in spite of a higher activity of NADH-methemoglobin reductase. The ATPase activity is doubled and ATP is presumably used for phosphorylation of membrane proteins, which leads to cross-linking of membrane proteins. This assumption could be supported by the observed decrease in non-electrolyte permeability, by increased binding of hemoglobin to the membrane, and polymerisation of membrane proteins detected by SDS-polyacrylamide gel electrophoresis. By means of electron microscopy, it could also be shown that the inclusion bodies are bound to the inner surface of membrane and cause its protrusion. This linkage might be responsible for the observed inhibition of the lateral movement of intramembrane particles.",
author = "J. Szel{\'e}nyi and G. Lelkes and M. Hor{\'a}nyi and J. F{\"o}ldi and I. Sz{\'a}sz and S. Holl{\'a}n",
year = "1981",
language = "English",
volume = "40",
pages = "961--967",
journal = "Acta Biologica et Medica Germanica",
issn = "0001-5318",
publisher = "Akademie Verlag GMBH",
number = "7-8",

}

TY - JOUR

T1 - Erythrocyte alterations in hemoglobin H disease

AU - Szelényi, J.

AU - Lelkes, G.

AU - Horányi, M.

AU - Földi, J.

AU - Szász, I.

AU - Hollán, S.

PY - 1981

Y1 - 1981

N2 - This study on erythrocytes in hemoglobin H (Hb-H) disease reveals that unstable Hb-H is bound to membranes to a greater extent, especially when it forms methemoglobin or is precipitated as an inclusion body. The methemoglobin content of these erythrocytes is elevated in spite of a higher activity of NADH-methemoglobin reductase. The ATPase activity is doubled and ATP is presumably used for phosphorylation of membrane proteins, which leads to cross-linking of membrane proteins. This assumption could be supported by the observed decrease in non-electrolyte permeability, by increased binding of hemoglobin to the membrane, and polymerisation of membrane proteins detected by SDS-polyacrylamide gel electrophoresis. By means of electron microscopy, it could also be shown that the inclusion bodies are bound to the inner surface of membrane and cause its protrusion. This linkage might be responsible for the observed inhibition of the lateral movement of intramembrane particles.

AB - This study on erythrocytes in hemoglobin H (Hb-H) disease reveals that unstable Hb-H is bound to membranes to a greater extent, especially when it forms methemoglobin or is precipitated as an inclusion body. The methemoglobin content of these erythrocytes is elevated in spite of a higher activity of NADH-methemoglobin reductase. The ATPase activity is doubled and ATP is presumably used for phosphorylation of membrane proteins, which leads to cross-linking of membrane proteins. This assumption could be supported by the observed decrease in non-electrolyte permeability, by increased binding of hemoglobin to the membrane, and polymerisation of membrane proteins detected by SDS-polyacrylamide gel electrophoresis. By means of electron microscopy, it could also be shown that the inclusion bodies are bound to the inner surface of membrane and cause its protrusion. This linkage might be responsible for the observed inhibition of the lateral movement of intramembrane particles.

UR - http://www.scopus.com/inward/record.url?scp=0019832336&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019832336&partnerID=8YFLogxK

M3 - Article

C2 - 6277117

AN - SCOPUS:0019832336

VL - 40

SP - 961

EP - 967

JO - Acta Biologica et Medica Germanica

JF - Acta Biologica et Medica Germanica

SN - 0001-5318

IS - 7-8

ER -