PMID: 3539183Oct 7, 1986Paper

Permissible discontinuity region of the alpha-chain of hemoglobin: noncovalent interaction of heme and the complementary fragments alpha 1-30 and alpha 31-141

Biochemistry
R SeetharamA S Acharya

Abstract

Generation of a fragment-complementing system of the alpha-chain on limited proteolysis with Staphylococcus aureus V8 protease has been investigated. Digestion of the alpha-chain (0.4 mM) of hemoglobin with V8 protease in phosphate buffer at pH 6.0 and 37 degrees C is limited to the peptide bonds of Glu-23, Glu-27, Glu-30, and Asp-47. Gel filtration of a V8 protease digest of the alpha-chain on a Sephadex G-50 column did not release any heme to the low molecular weight region, though some peptides were released from the protein. The filtration studies revealed the presence of two heme-containing components in the digest, the major one eluting at the alpha-chain position and the minor one eluting slightly ahead of the alpha-chain position. Reversed-phase high-performance liquid chromatography and amino-terminal sequence analysis demonstrated that the component eluting at the alpha-chain position contains species generated by the noncovalent interactions of heme and the complementary fragments alpha 1-30 and alpha 31-141. In dilute solutions (0.04 mM) the V8 protease digestion occurred exclusively on the carboxyl side of Glu-30(alpha). This high selectivity was also observed at pH 4.0 and pH 7.8. The visible spectra and the ultra...Continue Reading

References

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Citations

Mar 2, 2005·Biopolymers·Vadim T IvanovOleg N Yatskin
May 1, 1996·Protein Science : a Publication of the Protein Society·M J RaoA S Acharya
Dec 2, 1988·Biochimica Et Biophysica Acta·M C PeñaJ L Nieto
Oct 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·K S Iyer, A S Acharya
Sep 27, 1994·Proceedings of the National Academy of Sciences of the United States of America·A SharmaR Kumar
Apr 21, 2004·Protein Science : a Publication of the Protein Society·Sonati SrinivasuluSeetharama A Acharya

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