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The deficiency of a lysosomal acid hydrolase in two clones derived from the human lymphoblastoid line F137 after mutagen treatment
Author(s) -
GARDINER S. ELIZABETH,
SWALLOW DALLAS M.,
HARRIS HARRY,
ARTHUR ELIZABETH,
EVANS H. J.
Publication year - 1977
Publication title -
annals of human genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.537
H-Index - 77
eISSN - 1469-1809
pISSN - 0003-4800
DOI - 10.1111/j.1469-1809.1977.tb01958.x
Subject(s) - mutagen , clone (java method) , biology , enzyme , sandhoff disease , lymphoblast , genetics , hexosaminidase , lysosomal storage disease , microbiology and biotechnology , mutation , point mutation , karyotype , tay sachs disease , gene , chromosome , biochemistry , cell culture , dna , disease , medicine
SUMMARY Two clones (out of a total of 181 clones tested) derived from the human lymphoblastoid (lymphoid) line F137 after mutagen treatment were found to be deficient in a lysosomal acid hydrolase. The clone N32 derived from EMS‐treated F137 is deficient in N‐acetyl hexosaminidase A and B but contains normal levels of N‐acetyl hexosaminidase C and low levelsof an enzyme resembling N‐acetyl hexosaminidase S. Thus the enzyme deficiency in this clone appears to resemble the so‐called Sandhoff variant of Tay‐Sachs disease, a disease inherited as an autosomal recessive condition. The clone G3 derived from MNNG treated F137 is deficient in α‐galactosidase A. This clone resembles the situation in X‐linked Fabry's disease. Karyotype analysis of the clones failed to reveal any chromosome rearrangement or losses of chromosomal material that might have accounted for the mutations and it is suggested that a single point mutation might in each case account for the loss of enzyme activity. No storage of the natural substrates of the two enzymes could be demonstrated in the clones.