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ß-Galactosidase

AMINO- AND CARBOXYL-TERMINAL STUDIES

From the ¹ From the Department of Biological Chemistry, School of Medicine, University of California, Los Angeles, California 90024

ß-Galactosidase was analyzed for NH₂-terminal amino acids by the Sanger procedure. About two-thirds of a mole of threonine per 135,000 g was obtained, even with the use of dinitrophenyl-threonine-¹⁴C as internal control. The same result was obtained with protein treated by a variety of dissociating conditions before analysis. However, the Stark and Smyth carbamylation method yielded 1 mole of threonine per 135,000 g of protein. Labeled enzyme was prepared from a culture to which acetate-1-¹⁴C was added. Treatment with methanolic HCl and with Pronase showed that N-acetyl groups were absent from ß-galactosidase. Carboxypeptidase A released no amino acid from denatured protein. Carboxypeptidase B removed 1 mole of lysine per 135,000 g, and lysine was shown to be the only COOH-terminal amino acid when performic acid-oxidized and carboxymethylated ß-galactosidase were treated with carboxypeptidase B. The hydrazinolysis method also released lysine. On the basis solely of these end group studies, it seems possible that the ß-galactosidase monomer is a single long chain.

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