Synthetic potential of Staphylococcus aureus V8-protease: an approach toward semisynthesis of covalent analogs of alpha-chain of hemoglobin S

Journal of Cellular Biochemistry
R Seetharam, A S Acharya

Abstract

Enzyme-catalyzed reformation of peptide bonds in the noncovalent fragment systems of proteins has been emerging as a convenient procedure for the semisynthesis of covalent analogs of the respective proteins. Limited proteolysis of the alpha-chain of hemoglobin S with Staphylococcus aureus V8-protease converts the chain into a fragment-complementing system by hydrolyzing the peptide bond Glu(30)-Arg(31) of the chain. Therefore, it is conceivable that semisynthesis of covalent analogs of alpha-chain could be achieved if conditions for the V8-protease catalyzed formation of peptide bonds could be established. The synthetic potential of V8-protease has been now investigated by incubating V8-protease-derived fragments of alpha-chain, namely alpha 1-30 and alpha 31-47 with the enzyme at pH 6.0 in the presence of n-propanol as the organic cosolvent. RP high performance liquid chromatography analysis showed that a new chromatographically distinct component is generated on incubation, and this has been identified as alpha 1-47 by amino acid analysis, redigestion with V8-protease (in the absence of n-propanol), and tryptic peptide mapping. Optimal conditions for the synthesis of alpha 1-47 is at pH 6.0, 4 degrees C, and 24 hr of incubati...Continue Reading

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Jan 1, 1994·Peptides·J Bongers, E P Heimer
Oct 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·K S Iyer, A S Acharya
May 22, 2002·Protein Science : a Publication of the Protein Society·Sonati Srinivasulu, A Seetharama Acharya
Apr 21, 2004·Protein Science : a Publication of the Protein Society·Sonati SrinivasuluSeetharama A Acharya
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Mar 1, 1990·International Journal of Peptide and Protein Research·V De Filippis, A Fontana
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