Hexosaminidase (EC 22.214.171.124) activity from human liver and kidney extract was completely precipitated by anti-hexosaminidase A antiserum and 80 to 90% by anti-hexosaminidase B antiserum. Immunologically distinct hexosaminidase "C" could not be detected in these tissues. The final fractions of hexosaminidase A eluted from DE-52 chromatography were resolved into several enzymatically active components by rechromatography. Compared to hexosaminidase A and B, these minor components are more anodal in polyacrylamide disc electrophoresis. The residual activity of hexosaminidase from liver and fibroblasts of patients with Sandhoff's disease has also been resolved into similar components. The enzyme activity of these more anodal hexosaminidase components was precipitated completely by anti-hexosaminidase A antiserum and partially by anti-hexosaminidase B antiserum. The minor, more anodal components probably represent hexosaminidase molecules having an altered ratio of subunits or the degradation products of hexosaminidase A.
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