title: 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.
authors: Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Salamanca, Spain.
authors: J
authors: J
authors: Garcia-Alonso
authors: A
authors: A
authors: Reglero
authors: J A
authors: JA
authors: Cabezas
mesh_terms: D000665:Ampholyte Mixtures; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002852:Chromatography, Ion Exchange; D004795:Enzyme Stability; D012685:Sepharose / Q000031:analogs & derivatives; D013552:Swine; D001619:beta-N-Acetylhexosaminidases / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D000665:Ampholyte Mixtures; C028326:concanavalin A-sepharose; D012685:Sepharose; D001619:beta-N-Acetylhexosaminidases