JBC, Vol. 250, Issue 19, 7752-7758, Oct, 1975
Biochemical and immunological studies of purified mouse beta-galactosidase
S. Tomino and M. Meisler
Beta-Galactosidase (EC 3.2.1.23) has been purified from the livers of
C57BL/6J mice. The enzyme migrated as a single band of protein on
polyacrylamide gel electrophoresis in the presence of sodium dodecyl
sulfate. The molecular weight of the denatured and reduced enzyme was
63,000. The native form of beta-galactosidase appeared to be a tetramer of
240,000 at pH 5.0, which was reversibly dissociated at alkaline pH to a
dimer with apparent molecular weight of 113,000. Multiple charge isomers of
beta-galactosidase were resolved by polyacrylamide gel electrophoresis and
ion exchange chromatography. Treatment of beta-galactosidase with
neuraminidase markedly reduced its electrophoretic mobility. Purified
enzyme as well as crude liver extract hydrolyzed
p-nitrophenyl-beta-D-fucoside at one-tenth the rate of hydrolysis of the
beta-galactoside. Antiserum to the purified enzyme precipitated the major
portion of beta-galactosidase activity of mouse liver, brain, and kidney.
This antiserum cross-reacts with beta-galactosidases from rat and Chinese
hamster, but not with human, porcine, or bovine beta-galactosidase.
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