Literature DB >> 618877

Comparative studies of Hb Lepore Boston, Hb A2, and Hb A.

K Adachi, T Asakura, F M Gill, E Schwartz.   

Abstract

Several functional tests were performed to compare Hb A, Hb A2, and Hb Lepore Boston, which has a delta-beta crossover in the region of residues 87 to 116. Oxygen equilibrium curves determined by an automatic apparatus in 0.1 M potassium phosphate buffer, pH 7.0, at 20 degrees showed that the p50 was 5.8 mm Hg for Hb Lepore Boston, in contrast to 8.1 and 10.3 mm Hg for Hb A2 and Hb A, respectively. The n values (Hill coefficinets) of Hb Lepore Boston and Hb A2 were slightly smaller than that of Hb A. The effect of 2,3-diphosphoglycerate and inositolhexophosphate on the p50 of Hb Lepore Boston and Hb A2 was less than that on the p50 of Hb A. The molecular stability to mechanical shaking of Hb Lepore Boston and Hb A2 showed that the oxy forms of Hb Lepore Boston and Hb A2 denatured at a rate 3 times faster than that of Hb A. MetHb Lepore Boston was more unstable than MetHb A2 to mechanical shaking. These results indicate that, although the molecular stability of Hb Lepore Boston is more similar to that of Hb A2 than that of Hb A, the oxygen-binding properties of Hb Lepore differ from both Hb A and Hb A2.

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Year:  1978        PMID: 618877

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  1 in total

1.  Structural bases of the inhibitory effects of hemoglobin F and hemoglobin A2 on the polymerization of hemoglobin S.

Authors:  R L Nagel; R M Bookchin; J Johnson; D Labie; H Wajcman; W A Isaac-Sodeye; G R Honig; G Schilirò; J H Crookston; K Matsutomo
Journal:  Proc Natl Acad Sci U S A       Date:  1979-02       Impact factor: 11.205

  1 in total

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