doi: 10.1016/0020-711x(90)90043-3.
Purification and properties of beta-N-acetylhexosaminidase A from pig brain
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- PMID: 2143152
- DOI: 10.1016/0020-711x(90)90043-3
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Purification and properties of beta-N-acetylhexosaminidase A from pig brain
Int J Biochem.
1990.
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.
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