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Oxygen-linked CO2 binding to isolated beta subunits of human hemoglobin

Bauer, Christian and Kurtz, Armin (1977) Oxygen-linked CO2 binding to isolated beta subunits of human hemoglobin. The Journal of biological chemistry 252 (9), pp. 2952-2955.

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Abstract

It is known that most of the oxygen-linked carbamate which is formed in normal adult human hemoglobin (Hb A) is confined to the beta subunits rather than to the alpha subunits. In order to find out if similar differences exist in the isolated protomers of Hb A we have measured the effect of various pressures of carbon dioxide (pCO2) on the oxygen affinity in the following heme pigments: isolated ...

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Item type:Article
Date:1977
Institutions:Biology, Preclinical Medicine > Institut für Physiologie > Prof. Dr. Armin Kurtz
Identification Number:
ValueType
16010PubMed ID
Classification:
NotationType
AdultMESH
Carbamates/metabolismMESH
Carbon Dioxide/metabolismMESH
Chemical PhenomenaMESH
ChemistryMESH
Hemoglobin A/metabolismMESH
Hemoglobins/metabolismMESH
HumansMESH
Hydrogen-Ion ConcentrationMESH
Macromolecular SubstancesMESH
Myoglobin/metabolismMESH
OxygenMESH
Partial PressureMESH
Protein BindingMESH
Pyridoxal PhosphateMESH
Sulfhydryl CompoundsMESH
Dewey Decimal Classification:500 Science > 570 Life sciences
600 Technology > 610 Medical sciences Medicine
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Unknown
Item ID:27026
Owner only: item control page

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