The concept has been advanced that many enzymes are present in cells in at least two forms. The term "lyoenzyme" has been ascribed to the extractable component and "desmoenzyme" to the insoluble fraction which remained fixed to the cellular structural constituents (1-3). Lison (4) deserves credit for re-emphasizing the role of these two enzyme components in histochemical analysis. Investigators who have been developing or :employing histochemical techniques have been aware of the significant amount of enzyme which diffuses into the incubation medium. The appearance of the split product in the buffered substrate solution as well as in the tissue section has been a disturbing feature of many methods. Efforts to reduce this phenomenon have been partly successful by either exposing the tissues to fixatives before incubation, or by adding high concentrations of salts to the incubating solution. These attempts have met with varying degrees of success, depending to a large extent upon the enzyme being investigated, the degree of inhibition by these agents, and the solubility characteristics of the enzyme. Although a marked decrease in the amount of enzyme diffusing into the incubation solution may be attained under certain conditions, the extent of the movement of the enzyme within the cell and the exact amount of diffusion out of the tissue section is still undetermined.In recent years, Several quantitative methods have been employed in enzyme histochemistry, but these were not specifically designed to measure the lyo and desmo components of enzymes.
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