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Examination of residual enzyme activity in patients' liver, kidney, leukocytes and fibroblasts showed a generalized, heritable defect: the apparent<jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> for glycerol was increased 5\u2010200\u2010fold over control values, whereas the apparent<jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> for ATP was not significantly altered. This kinetic defect was similar in fibroblasts from clinically different individuals with this inborn error of metabolism. Hybridization of fibroblasts from these individuals showed no evidence of complementation for glycerol kinase activity.<\/jats:p>","DOI":"10.1007\/bf02179133","type":"journal-article","created":{"date-parts":[[2005,9,20]],"date-time":"2005-09-20T20:30:13Z","timestamp":1127248213000},"page":"177-182","source":"Crossref","is-referenced-by-count":19,"title":["Human glycerol kinase deficiency: Enzyme kinetics and fibroblast hybridization"],"prefix":"10.1002","volume":"5","author":[{"given":"E. 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