Abstract
Abstract Carboxypeptidase digestion of denatured thiogalactosidase transacetylase showed that the COOH-terminal sequence is Ser-Val and that 2 moles of valine are released per mole of protein. Although this is consistent with the previous finding that the protein is composed of two identical chains, studies of the NH2 terminus show heterogeneity and lack of stoichiometry. Instead of 2 moles of a single amino acid per mole of protein, 0.5 mole of aspartic acid (or asparagine) and 0.4 mole of methionine were found by both the Sanger and the Stark and Smyth procedures. The same result was obtained after treatment of the protein under conditions expected to cleave α-N-formyl groups. Various explanations to account for these findings are discussed, including blocked NH2-terminal end groups, proteolytic hydrolysis, and random cleavage as a consequence of a step in protein biosynthesis.
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