Identification of a distinctive molecular form of alcohol dehydrogenase in human livers with high activity
Human liver alcohol dehydrogenase activity and isoenzyme pattern have been compared in specimens from different sources. Specific enzymatic activity was significantly higher in surgical biopsy samples than in autopsy specimens. Furthermore, tissues from individuals who died suddenly from trauma exhibited significantly higher activities than those obtained following disease-related deaths. All livers with high specific activity revealed on starch gel electrophoresis, in addition to the usual isoenzymes, a prominent, previously unrecognized, activity band. This molecular form, more anodic than the others at pH 8.6 and 7.7, was separated by isoelectric focusing. It exhibited kinetic properties characteristic of the alcohol dehydrogenase isoenzymes. © 1975 Academic Press, Inc.
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