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Interrelation between high molecular weight and low molecular weight forms of gm 1 beta galactosidase ec purified from porcine spleen

Interrelation between high molecular weight and low molecular weight forms of gm 1 beta galactosidase ec purified from porcine spleen

Journal of Biochemistry 92(1): 13-22

ISSN/ISBN: 0021-924X

Two forms of acid .beta.-galactosidase [EC] with different MW catalyzing the hydrolysis of GM1-ganglioside and p-nitrophenyl-.beta.-D-galactoside were separated and purified from porcine spleen. The apparent MW were 400,000-600,000 and 70,000-74,000 for the high (termed Am form) and low (termed A1 form) MW forms, respectively. On examination by sodium dodecyl sulfate (SDS)/polyacrylamide gel electrophoresis, both forms of the enzyme had a common protein band of MW 63,000 and the Am form showed 3 additional protein bands with MW of 31,000, 21,000 and 20,000. Both forms of the enzyme had similar catalytic functions with regard to pH optimum, Km, substrate specificity, and sensitivity to substrate analogs and other substances such as detergents, bovine serum albumin (BSA) and NaCl. Both forms of the enzyme were fairly stable upon preincubation at C at acidic pH (4.5) but lost their activities at neutral pH (7.0). The A1 form was a monomer at neutral pH (7.0) and formed a dimer at acidic pH (4.5). However, most of the Am form could not be converted to a dimeric form on gel filtration at acidic pH.

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Accession: 005733011

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