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J. Biochem, 1968, Vol. 63, No. 2 186-192
© 1968 Japanese Biochemical Society

research-article

Studies on Enzymes Acting on Glycopeptides*

MAYUMI MAKINO, TOSHIMASA KOJIMA, TADAYASU OHGUSHI and IKUO YAMASHINA**

From the Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University Kyoto

1. An enzyme, tentatively named glycopeptidase, was found in blood serum and tissues. This enzyme degraded synthetic ß-aspartylglycosylamine and an ovalbumin glycopeptide to yield aspartic acid, ammonia and N-acetylglucosamine (or an oligosaccharide with N-acetyl-glucosamine at the reducing terminal).

2. Glycopeptidase was found to hydrolyze the amide bond of ß-aspartylglycosylamine producing glycosylamine, while the glycosylamine was subsequently hydrolyzed non-enzymatically.

3. Glycopeptidase appeared to require for its action both {alpha}-amino and {alpha}-carboxyl groups of aspartic acid linked to carbohydrate.

4. A glycosylamine, 1-amino-N-acetylglucosamine, was synthesized and fully characterized in the identification of the product of glycopeptidase action on synthetic ß-aspartylglycosylamine.

* Support was provided by a grant from the Ministry of Education, Japan.

** Inquiries should be sent to Dr. I. Yamashina


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