Purification and properties of beta-N-acetylhexosaminidase A from pig brain

Abstract

1. Adult pig brain beta-N-acetylhexosaminidase was separated into four different forms by ion exchange chromatography on diethylaminoethyl-cellulose. 2. Form A was purified 1300-1500 fold by an unusual procedure, the technique of ampholyte displacement, followed by chromatography on concanavalin A Sepharose. 3. The enzyme catalyses the hydrolysis of both beta-N-acetylglucosaminides and beta-N-acetylgalactosaminides. 4. The kinetic studies support the evidence of the association of both activities to a single protein, and at the same active site. 5. A natural substrate, N,N'-diacetylchitobiose, is also hydrolyzed, but not ovalbumin. 6. This enzyme may be considered as an exoglycosidase.