منابع مشابه
Fetal Hemoglobin with Abnormal ‘ Y . Polypeptide Chains : Hemoglobin Warren
By T. H. J. HUISMAN, A. M. Dozy, B. E. HORTON AND J. B. WILsON T HE EXISTENCE of variants of normal human fetal hemoglobin ( HbFor a2y2 ) has been suggested in different reports in the literature. Variants of fetal hemoglobin with abnormal a-polypeptide chains have been described5 ”5 and some are well characterized.’0 Only one abnormality, namely the electrophoretically fast moving hemoglobin v...
متن کاملAssembly of the peptide chains of hemoglobin.
* This res/arch was supported by a grant from The Commonwealth Fund, Grant No. H2042(C3) from the National Heart Institute, aada grant from the National Science Foundation. 1 Fisher, H. F., E. E. Conn, B. Vennesland, and F. H. Westheimer, J. Biol. Chem., 202, 687 (1953). 2 Hoewus, F. A., F. H. Westheimer, and B. Vennesland, J. Am. Chem. Soc., 75, 5018 (1953). ' Singer, T. P., and E. B. Kearney,...
متن کاملDifferent Properties of Ferrous Iron in Deoxygenated Hemoglobin Chains
— Iron 57-enriched, deoxygenated human (adult) hemoglobin (HbA), its isolated asHand /?sn-chains, and the partially iron 57-enriched, fully functional hemoglobin a2(Fe) j82(Fe) were investigated by Mossbauer spectroscopy in the temperature range 4.2 K-200 K. According to our experimental accuracy ( ± 0.006 mm s) the temperature dependent quadrupole splittings &EQ(T) of deoxygenated HbA, <XSHand...
متن کاملHeterotropic interactions in Monomeric (IS” Chains from Human Hemoglobin
The O2 affinity of fiSH chains is lowered by H+, inositol hexaphosphate (IHP), and COz. As the oxygen affinity of gSH monomers (flISH) is lower than that of fiSH tetramers (@dSH), it is possible that IHP and CO2 exert their influence on the Oz affinity of PSH chains by increasing the dissociation constant of +3dsH rather than by a direct effect on the molecule. In order to test for this hypothe...
متن کاملInhibition of the biosynthetic completion of rabbit hemoglobin by isolated human hemoglobin chains.
A cell-free system from rabbit reticulocytes incorporated i4C-valine and 14C-leucine into hemoglobin. This synthesis of rabbit hemoglobin was inhibited in a specific manner when (Y or /3 chains, isolated from human hemoglobin, were added to the system. The human cy and /3 chains interacted with the newly synthesized ‘C-rabbit chains to form hybrid hemoglobins, which were identified by cellulose...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)44362-7