IOVS Am. J. Clin. Nutrition
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(Investigative Ophthalmology and Visual Science. 1971;10:887-897.)
© 1971 by The Association for Research in Vision and Ophthalmology, Inc.

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Glycosidases of the Crystalline Lens

I. Effect of pH, Inhibitors, and Distribution in Various Areas of the Lens and in Subcellular Fractions

RICHARD CARLIN 1 and EDWARD COTLIER 1

1 Department of Ophthalmology, University of Illinois Eye and Ear Infirmary, University of Illinois at the Medical Center, Chicago, Ill.

Six glycosidases, enzymes involved in glycoprotein-glycolipid breakdown, were determined in human, rabbit, and rat crystalline lens: {beta}-galactosidase, {beta}-glucosidase, {alpha}-mannosidase, {beta}-glucosaminidase, {beta}-galactosaminidase, and {beta}-fucosidase. Peak activities of these enzymes were all at acidic pH values, but individual variations in pH optimum among enzymes and species were present. In the rabbit, glycosidase activities were 11 to 29 times higher in lens than in aqueous humor. In determinations in various areas of the lens, glycosidase activities were higher in the capsule-epithelium area than in the rest of the lens (on a wet iveight basis). A variety of steroids inhibited {beta}-glucosidase, whereas vitamin A palmitate stimulated {beta}-glucosidase and {beta}-fucosidase.

Key Words: crystalline lens • {beta}-galactosaminidase • {beta}-glucosidase • {alpha}-mannosidase • {beta}-glucosaminidase • {beta}-galactosaminidase • {beta}-fucosidase

Submitted on June 30, 1971
Accepted on September 21, 1971




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