Further Studies on the Oxygen Equilibrium of Hemoglobin

Allen, David W.; Guthe, Karl F.; Wyman, Jeffries

doi:10.1016/s0021-9258(19)50965-6

Cited by 161 publications

(10 citation statements)

References 6 publications

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“…We now ask how the hemes may be oriented with respect to the --SH clusters. Allen, Guthe, and Wyman (1950) have concluded that the heroes in normal hemoglobin must all be indistinguishable from one another, that each of the four hemes is bound in the same way to the protein, and that they are all identical in their interactions. We shall assume these conclusions to be correct for horse hemoglobin.…”

Section: Discussionmentioning

confidence: 99%

Sulfhydryl Groups and the Structure of Hemoglobin

Riggs

Wolbach

1956

The Journal of General Physiology

245

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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 p50). Mersalyl and mercuric chloride at this concentration each increase the oxygen affinity, while PCMB and methyl mercury have little or no effect on the oxygen affinity. These effects are primarily associated with the binding of —SH groups, and are largely reversed on the addition of glutathione. —SH groups do not appear to be responsible for the Bohr effect. 2. Evidence is presented for the belief that the two hemes of each half-molecule of horse hemoglobin are situated on either side of a cluster of—SH groups. 3. The mechanism of interaction between the hemes is discussed. It is concluded that the reorganization of the protein architecture which accompanies oxygenation plays a central role in this interaction, in agreement with the views of Pauling and Wyman.

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Section: Discussionmentioning

confidence: 99%

Sulfhydryl Groups and the Structure of Hemoglobin

Riggs

Wolbach

1956

The Journal of General Physiology

245

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“…Oxygen equilibria were determined by minor modifications of the method of Allen et al, (1950), andRiggs (1951) on electrophoretically isolated (Kunkel et al, 1957) Hb A and Hb Chesapeake. The nitrogen used for deoxygenation was freed of 02 by the method of Meites and Meites (1948).…”

Section: Methodsmentioning

confidence: 99%

Relation between Structure and Function in Hemoglobin Chesapeake^*

Nagel¹,

Gibson²,

Charache³

1967

Biochemistry

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“…The shape of the 02 saturation curve for human hemoglobin was found by Allen et al (1950) and by Roughton (1964) to be unaffected by pH except for possible deviations at very low or very high fractional saturations. This invariance with pH implies that each step of the reaction process is similarly affected by pH.…”

Section: Discussionmentioning

confidence: 90%