Ferricyanide reductase activity in cataractous human lens.
We assayed ferricyanide reductase activity (one of NADH-dependent diaphorase activities) in the soluble and insoluble fractions of cataractous human lenses. Activity of this reductase in both the soluble and insoluble fractions tended to decrease in order of cortex > nucleus periphery > nucleus center, and it was suggested that a decrease of the reductase activity is closely correlated with lens protein aggregation, and to some extent associated with the development of nuclear sclerosis (coloration) and cortical cataract. Furthermore, insoluble fraction had very high specific activity per mg insoluble protein in cortex, and the activity decreased sharply with an increase in the level of insoluble protein. The reductase activity in the insoluble fraction may be also related to the metabolic activity of plasma membranes.
Matsukura
S
S
Department of Ophthalmology, Tokai University School of Medicine, Kanagawa, Japan.
Bando
M
M
Obazawa
H
H
D000368:Aged; D000369:Aged, 80 and over; D002386:Cataract / Q000201:enzymology*; D006801:Humans; D007904:Lens Cortex, Crystalline / Q000201:enzymology*; D007907:Lens Nucleus, Crystalline / Q000201:enzymology*; D008875:Middle Aged; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism; D012995:Solubility
D009247:NADH, NADPH Oxidoreductases; C014227:ferricyanide reductase