SULFHYDRYL GROUPS AND THE STRUCTURE OF HEMOGLOBIN
نویسندگان
چکیده
منابع مشابه
Sulfhydryl Groups and the Structure of Hemoglobin
1. Addition of 2 moles of mersalyl, mercuric chloride, p-chloromercuribenzoate (PCMB), or methyl mercury hydroxide per mole of hemoglobin greatly reduces heme-heme interactions (n), yet these substances have quite different effects on the oxygen affinity (-log p(50)). Mersalyl and mercuric chloride at this concentration each increase the oxygen affinity, while PCMB and methyl mercury have littl...
متن کاملSulfhydryl Groups and the Structure of Hemoglobin by Austen
Hemoglobins possess two very striking properties: they combine reversibly with oxygen, and this binding appears to be autocatalytic. Each molecule of vertebrate hemoglobin possesses four heine groups which combine reversibly with oxygen, and are so associated that the binding of oxygen by one heine greatly enhances the affinity of a second heine for oxygen. Two closely related proposals have be...
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15 صفحه اولSulfhydryl Groups and the Interaction between the Hemes in Hemoglobin
1. Dialysis of a hemoglobin solution against slightly alkaline buffer (pH 8.68) causes a decrease in heme-heme interaction. The value of n in Hill's equation drops from 2.9 to 2.0, while the oxygen affinity increases slightly. Addition of glutathione largely reverses the effects of dialysis (n rises from 2.0 to 2.5 to 2.6). 2. Addition of the sulfhydryl reagent, p-chloromercuribenzoate (1.8 x 1...
متن کاملThe Reactions of the Sulfhydryl Groups of Human Hemoglobin &*
The rates at which the sulfhydryl groups on each chain of hemoglobin fi4 react with N-ethylmaleimide and iodoacetate have been measured. The sulfhydryl group at position 93 reacts with both alkylating agents at approximately the same rate as normal liganded hemoglobin. The sulfhydryl group at position 112, which is not available in normal hemoglobin, reacts in hemoglobin f14 and does so much mo...
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ژورنال
عنوان ژورنال: Journal of General Physiology
سال: 1956
ISSN: 1540-7748,0022-1295
DOI: 10.1085/jgp.39.4.585