Assay conditions were studied for eight lysosomal
enzymes in lymphoblastoid cell lines transformed by Epstein-Barr virus. The transformed lymphoblastoid cells retained all eight
enzyme activities, though the levels sometimes differed from those in the peripheral lymphocytes or granulocytes. The levels of these eight lysosomal
enzymes were measured in lymphoblastoid cells from 11 patients with hereditary
lysosomal storage diseases--GMI-
gangliosidosis, a variant of
beta-galactosidase deficiency (
sialidase deficiency with a partial
beta-galactosidase deficiency),
Tay-Sachs disease,
Gaucher disease,
Hurler syndrome,
Scheie syndrome and
I-cell disease--and from 20 of their obligate heterozygotes. No activity of
enzymes that were deficient in the respective disease, except
I-cell disease, was detected in the lymphoblastoid cells from the patient. In
I-cell disease, the cells showed lower levels of some
enzyme activities.
beta-D-Galactosidase activity from heterozygotes of the patient with GMI-
gangliosidosis and
alpha-L-iduronidase activity from heterozygotes of the patient with
Hurler syndrome were in carrier range. On
sephadex G-150 gel filtration,
beta-D-galactosidase in control material gave two peaks (I and II). In GMI-
gangliosidosis, peak II was absent and peak I was markedly diminished. Peak II in the heterozygotes was smaller than that of control. On
DEAE cellulose column chromatography of
hexosaminidase, two major
isoenzymes (
hexosaminidase A and B) were detected in control. However,
hexosaminidase A was not detected in
Tay-Sachs disease, and the ratios of
hexosaminidase (
Hex) A/
Hex B in the parents were lower than those in control.