Heterogeneity of Beta-Galactosidase from Rabbit Spleen

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Abstract
Two forms, I and II, of an acid ß-galactosidase from rabbit spleen were separated by DEAE-cellulose chromatography and then characterized. Both forms of the enzyme showed different heat-stability (form I being heat-labile and form II heat-stable), and different pi (6.7 for form I and 5.3 and 6.7 for form II). Their gel filtration patterns were also different: form I was resolved in a single peak of mol. wt. 75,000, whereas form II was resolved in one or two peaks of mol. wt. 120,000 and greater than 200,000, depending on the pH of elution. However, both forms had similar pH stability and behavior toward α-methyl-ß-D-galactopyranoside, α-methyl-ß-D-glucopyranoside, urea and KC1. Differences in pH optima, optimal temperature and K(m) values were not marked.

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