Hemoglobin Abruzzo (beta143 (H21) His replaced by Arg). Consequences of altering the 2,3-diphosphoglycerate binding site
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Hemoglobin Abruzzo [ 0143 ( H 21 ) His - t Arg ] CONSEQUENCES OF ALTERING THE 2 , 3 - DIPHOSPHOGLYCERATE BINDING SITE
Hemoglobin Abruzzo is an abnormal human hemoglobin with a substitution at a residue known to be involved in the binding of 2,3-diphosphoglyceric acid. It has increased oxygen affinity and reduced heme-heme interaction in the absence of organic or inorganic phosphate cofactors. In inorganic phosphate buffers the Bohr effect and heme-heme interaction are normal, but the oxygen affinity remains hi...
متن کاملHemoglobin Rahere , A Human Hemoglobin Variant with Amino Acid Substitution at the 2 , 3 - Diphosphoglycerate Binding
We encountered an abnormal hemoglobin (Rahere), with a threonine residue replacing the ,682 (EF6) lysine residue at the binding site of 2,3-diphosphoglycerate, which was responsible for overt erythrocytosis in two individuals of a Japanese family. Hemoglobin Rahere shows a lower oxygen affinity on the binding of 2,3-diphosphoglycerate or chloride ions than hemoglobin A. Although a decrease in t...
متن کاملDiphosphoglycerate and inosine hexaphosphate control of oxygen binding by hemoglobin: a theoretical interpretation of experimental data.
A theoretical equation is presented for the control of cooperative adsorption on proteins and other linear macromolecules by hormones, drugs, ATP, and other "cardinal adsorbents." With reasonable accuracy, this equation describes quantitatively the control of oxygen binding to hemoglobin by 2,3-diphosphoglycerate and by inosine hexaphosphate.
متن کاملCharacterization and oxygen binding properties of des-Arg human hemoglobin.
The role of chloride in the stabilization of the deoxy conformation of hemoglobin (Hb), the low oxygen affinity state, has been studied in order to identify the nature of this binding. Previous studies have shown that arginines 141alpha could be involved in the binding of this ion to the protein. Thus, des-Arg Hb, human hemoglobin modified by removal of the alpha-chain C-terminal residue Arg141...
متن کاملCalorimetric Studies of Hemoglobin Function , the Binding of 2 , 3 - Diphosphoglycerate and Inositol Hexaphosphate to Human Hemoglobin
Calorimetric titration curves demonstrate the heat of binding of organic phosphates to oxyand deoxyhemoglobin at pH 7.4 in 0.05 M 2,2-bis(hydroxymethyl)-2,2’,2”-nitriloethanol buffer and 0.1 M Cl-. An absence of binding heat was noted at this pH value for both the 2,3-diphosphoglycerate (2,3-DPG) and inositol hexaphosphate (IHP) interactions with oxyhemoglobin. At pH 6.0, an exothermic heat of ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1975
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)41061-2