Crystallizable Recombined Hæm-Globin from Human Red-Cell Hæmoglobin

Jope, E. M.; Jope, H.M.; O'Brien, J.R.

doi:10.1038/164622b0

Cited by 31 publications

(10 citation statements)

References 5 publications

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“…The instability of globin preparations is well known (see, for example, Holden and Freeman, 1928;Mirsky and Anson, 1936). An aqueous solution of native globin prepared by the method of lope, Jope, and O'Brien (1949) is relatively stable at 0°C. However, rapid flocculation occurs if the temperature rises to 20°C.…”

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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“…Since then it has been clearly demonstrated that there are many important differences between human and animal and between foetal and adult haemoglobins (Kroger, 1888;Bischoff and Schulte, 1926;Haurowitz, 1930Haurowitz, , 1935Trought, 1932; Brinkman, Wildschut and Wittermans, 1934; Hill, 1935;Brinkman and Jonxis, 1935;Jope and O'Brien, 1949).Haselhorst and Stromberger (1930Stromberger ( , 1932 showed that the blood of the human foetus possessed a higher affinity for oxygen than that of its mother, but Hill (1935) found that human foetal haemoglobin had a lower affinity than human adult haemoglobin. This apparent anomaly was explained by the work of McCarthy (1943), who showed that the affinity of the haemoglobins for oxygen was greatly modified when they were within a corpuscle.…”

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confidence: 99%

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Haemoglobin and Red Cells in the Human Foetus: III. Foetal and Adult Haemoglobin

Walker¹,

Turnbull²

1955

Archives of Disease in Childhood

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In 1866 Korber found chemical differences between haemoglobin obtained from human placental blood and that from normal adult blood. Since then it has been clearly demonstrated that there are many important differences between human and animal and between foetal and adult haemoglobins (Kroger, 1888;Bischoff and Schulte, 1926;Haurowitz, 1930Haurowitz, , 1935Trought, 1932; Brinkman, Wildschut and Wittermans, 1934; Hill, 1935;Brinkman and Jonxis, 1935;Jope and O'Brien, 1949).Haselhorst and Stromberger (1930Stromberger ( , 1932 showed that the blood of the human foetus possessed a higher affinity for oxygen than that of its mother, but Hill (1935) found that human foetal haemoglobin had a lower affinity than human adult haemoglobin. This apparent anomaly was explained by the work of McCarthy (1943), who showed that the affinity of the haemoglobins for oxygen was greatly modified when they were within a corpuscle. Adult corpuscles caused a marked decrease in the oxygen affinity of their contained haemoglobin, while foetal corpuscles had little effect on the affinity of foetal haemoglobin for oxygen. Recently, Allen, Wyman and Smith (1953) have re-studied the oxygen affinity of human haemoglobins. Unlike Hill (1935) and Haurowitz (1935) they found no difference between the affinity for oxygen of the haemoglobin of the human foetus and that of its mother, provided that the haemoglobin solutions were so treated that the concentrations of dialysable substances were identical. They also found that the haemoglobin from one foetus at 31 weeks had the same affinity as the haemoglobins of term foetuses and of their mothers.Most investigators have been concerned with a study of the physical, chemical and other characteristics of human haemoglobins, and little information is available of the relative proportions of each type of haemoglobin in the blood of the human foetus at various stages of gestation, although such information is available for the sheep foetus. Karvonen (1949) found that adult haemoglobin first appeared in the sheep foetus at or about the 105th day and that at term 50% of the haemoglobin was adult in type. Beaven, Hoch and Holiday (1951), in one human foetus, at 20 weeks' gestation, found that 6 % of the haemoglobin was of the adult type and Schulman (1953) that there was at least 10% adult haemoglobin in the blood of premature infants. Many investigators have, however, studied the proportion of adult haemoglobin in the cord blood of the foetus at birth, at or near full term, and their results are shown in Table 1, from which it can be seen that

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“…The reading of the optical density at 280 nm corresponds to the concentration of peptides and amino acids in the permeate [25]. The reading of the optical density at 400 nm corresponds to the content of heam peptides in the permeate [26]. The permeate optical density is directly measured without pre-treatment.…”

Section: Measurement Of the Peptide Concentrationmentioning

confidence: 99%