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Distribution and Properties of Human Alcohol Dehydrogenase Isoenzymes
Efficient affinity and ion-exchange chromatographic methods have been developed for the purification and separation of all the alcohol dehydrogenase forms now known to exist. The kinetic properties of the major enzyme forms and the structural interrelations among them have been characterized. These...
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Published in: | Annals of the New York Academy of Sciences 1987, Vol.492 (1), p.1-10 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Efficient affinity and ion-exchange chromatographic methods have been developed for the purification and separation of all the alcohol dehydrogenase forms now known to exist. The kinetic properties of the major enzyme forms and the structural interrelations among them have been characterized. These studies as well as recent reports of the amino acid and cDNA sequences of different ADH subunits support the existence of at least five different structural genes for human ADH, three of which encode very closely related protein subunits. It is remarkable that the different isoenzymes of human ADH, differ so strikingly in catalytic properties. This paper summarizes some of the recent advances in this area fo knowledge. |
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ISSN: | 0077-8923 1749-6632 |
DOI: | 10.1111/j.1749-6632.1987.tb48648.x |