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J. Biochem, 1974, Vol. 76, No. 4 765-769
© 1974 Japanese Biochemical Society

research-article

Mode of Action on Proteins of Acid Carboxypeptidase from Aspergillus saitoi

Teruyoshi ARAI* and Eiji ICHISHIMA**

Laboratory of Microbiology and Enzymology, Tokyo Noko University Fuchu, Tokyo 183

**To whom inquires about this paper should be addressed

Acid carboxypeptidase [EC 3.4.12.1 [EC] ] isolated from the culture filtrate of Aspergillus saitoi has been investigated for its use in the carboxy-terminal sequence determination of native or reduced S-carboxymethyl-lysozyme and reduced S-carboxymethyl-ribonuclease at pH 2.5.

The sequence of the first four carboxy-terminal residues of denatured lysozyme, leucine, arginine, S-carboxymethyl-cysteine, and glycine, could be deduced unequivocally from a time release plot of an incubation mixture with the enzyme. The enzyme catalyzed the release of a small amount of leucine from native lysozyme in citrate buffer, pH 2.2, containing a small amount of the surface active agent Brij-35.

The first five residues, valine, serine, alanine, aspartic acid, and phenylalanine, were liberated rapidly from the carboxy terminus of reduced S-carboxymethyl-ribo-nuclease. A small amount of proline, which occupies position eight from the carboxy terminus, can be detected only after prolonged incubation for 20.5 hr.

*Present address: Tokyo Metropolitan Research Laboratories of Hygiene, Tachikawa, Tokyo.


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