Abstract
The molecular weights and subunit compositions of bovine liver β-acetylhexosaminidase A (Hex) and B (Hex B) were studied using enzyme preparations purified by octyl Sepharose chromatography. Analysis by gel filtration showed that Hex A had a molecular weight of ca. 310000 (hexamer) at pH 5, 6, and 6.5, and was dissociated into dimers at pH 7 and 8, while the molecular weight of Hex B, ca. 310000, remained constant in the pH range of 5-8. The molecular weights of Hex A and B subunits as determined by electrophoresis in sodium dodecyl sulfate were both ca. 52000, and this value remained unaltered when the enzyme was treated with a reducing agent or denaturant.
