Sorbitol Dehydrogenase In Human Lens: Study Of The Enzyme In Various Human Tissues View Full Text


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Article Info

DATE

1987-08

AUTHORS

K Schmid, B Kruis, W Endres, B Lorenz, Y S Shin

ABSTRACT

Several patients with congenital cataracts were described to have a deficient sorbitol dehydrogenase activity in erythrocytes (Human Genet. 61:338, 1982; J. Inner. Metab. Dis. 7 Suppl.2:151, 1984). Since there were obscure findings concerning the erythrocyte enzyme activity and the inheritance, we have studied the enzyme in lens and compared its property with that in other tissues such as liver and blood. The specific activity of sorbitol dehydrogenase in lens was higher than in liver (4.9-5.4 nmol/min/mg protein vs. 2.9-4.2 n=8 each). The Michaelis constant for sorbitol was low in lens compared to that in other tissues (0.9 nmol/L in lens, 2.6 mmol/L in liver). Polyacrylamide gel iso-electrofocusing of the enzyme in lens showed multiple bands between pH 4.4-8.1, while in liver 2-4 bands at pH 7.0-8.6 and in erythrocytes 3-4 bands at pH 7.6-8.4. Xylitol inhibited the enzyme in all samples studied by 30-50 %, whereas xylulose activated the enzyme by 200% in liver, in lens and erythrocytes by 40-60 %. These results indicate that sorbitol dehydrogenase in lens is unique compared with that in liver or erythrocytes. More... »

PAGES

237

Identifiers

URI

http://scigraph.springernature.com/pub.10.1203/00006450-198708000-00144

DOI

http://dx.doi.org/10.1203/00006450-198708000-00144

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1029393133


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