DISTRIBUTION OF SUBSTRATE-SPECIFIC ALKALINE PHOSPHATASES IN THE OCULAR TISSUES

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Abstract
PREVIOUS work from this laboratory (Maengwyn-Davies, Friedenwald, and White1) has shown that it is possible to demonstrate histochemically in fresh frozen tissue a group of substrate-specific enzymes which hydrolyze various phosphate esters in an alkaline environment. The methods devised give information as to the identity of the enzymes which are tested and also as to their location in the tissues. In the present study these methods have been applied to the ocular tissues. The fact that different tissues in a structure as highly organized as the eye have different complements of enzymes is hardly surprising. No doubt the variety of enzyme composition in different cells is an expression of their varied metabolic activities and of the metabolic interactions which contribute to organ functions. Maengwyn-Davies found that in an alkaline environment two enzyme systems attack the polyglycol monophosphate esters glycerophosphate, glucose-1-phosphate, glucose-6-phosphate, and fructose-6-phosphate. The A system, which is active

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