Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0086543 (cataract)
 29,165 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The isoelectric point distribution of G-3-P DH and TPI from human lenses was examined as a function of age and cataract formation. Both enzymes exhibited progressive heterogeneity with age and a shift towards an acidic charge. Little qualitative differences in the pI profiles of G-3-P DH and TPI were found to distinguish mixed cataracts from age comparable normal lenses. While the most alkaline form of G-3-P DH required less HAsO4= for optimal activity, no other kinetic property, i.e. Km substrate, cofactor and inhibitors distinguished any of the charge forms of G-3-P DH. All metaor isozyme forms of TPI had the same Km substrate in the forward and reverse reaction direction. The most acidic forms of G-3-P DH and TPI were less stable to increased temperatures than their more alkaline counterparts suggesting a decreased stability.
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PMID:Human lens enzyme alterations with age and cataract: glyceraldehyde-3-P dehydrogenase and triose phosphate isomerase. 395 39