1. A previously uncharacterized form of human liver acid beta-galactosidase (EC 188.8.131.52), possibly a dimer of molecular weight 160 000, was resolved by gel filtration. It has the same ability to hydrolyse GM1 ganglioside as the two other acid beta-galactosidase forms. 2. The low-molecular-weight forms of acid beta-galactosidase undergo salt-dependent aggregation. 3. The high-molecular-weight component may consist of the low-molecular-weight forms bound to membrane fragments. It can be converted completely into a mixture of these forms. 4. The neutral beta-galactosidase activity can be resolved into two forms by DEAE-cellulose chromatography. They differ in their response to Cl-ions. 5. A new nomenclature is suggested for the six beta-galactosidases so far found in human liver. 6. The enzymic constituents of the beta-galactosidase bands resolved by electrophoresis were re-examined. The A band contains three components. A two-dimensional electrophoretic procedure for resolving the A band is described. 7. The effect of neuraminidase treatment on the behaviour of beta-galactosidases in various separation systems is examined.
Research Article|July 01 1976
The separation and characterization of the methylumbelliferyl β-galactosidases of human liver
Biochem J (1976) 157 (1): 189-195.
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P S Cheetham, N E Dance; The separation and characterization of the methylumbelliferyl β-galactosidases of human liver. Biochem J 1 July 1976; 157 (1): 189–195. doi: https://doi.org/10.1042/bj1570189
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