Abstract
Enzymes associated with protein breakdown have been investigated in the human lens. A neutral proteinase has been found with properties similar to the bovine lens enzyme (Blow, van Heyningen and Barrett, 1975). It is maximally active at pH 7·5, stable for many hours at 55°C, activated by Mg 2+ and Ca 2+ and inhibited by EDTA. It is active against bulk human lens proteins and bovine lens α-crystallin but has little or no activity against haemoglobin, azocasein or bovine plasma albumin. The neutral proteinase appears to be the main, or only, proteinase in the normal and cataractous human lens; we were unable to find the proteinase with maximal activity at pH 5·2 described by Swanson and Nichols (1971). Neither leucine aminopeptidase nor carboxypeptidase A activity could be detected in the human lens.
Published Version
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