Abstract
Human erythrocyte Ca 2+-dependent neutral proteinase catalyzes a limited proteolysis of isolated globin chains. The rate of hydrolysis is very rapid using heme-deprived α- or β-globin chains and is reduced to one-fifth with their corresponding native forms. In both cases, the proteinase specifically cleaves a single peptide bond, this resulting in the removal from the amino-terminus end of an octapeptide in β-globin and of an undecapeptide in α-globin. Both peptides have been isolated, their amino acid composition has been characterized and the susceptible site of cleavage has been identified. Hemoglobin variants show a different rate of digestion as compared to that of normal chains. The α-Hasharon [α47(CES) Asp → His] undergoes rapid digestion, while the β-G San Josè chain [β7(A4) Glu → Gly], which carries the mutation near the site of cleavage, reveals a high degree of resistance to proteolytic degradation by the neutral proteinase.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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