HISTOCHEMICAL DEMONSTRATION OF OXIDATIVE ENZYMES IN THE ADENOHYPOPHYSIS OF THE PIG, WITH PARTICULAR REFERENCE TO THE PARS INTERMEDIA

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Abstract
SUMMARY: The adenohypophysis of the pig was examined histochemically for the presence of 11 oxidative enzymes, namely: 1.1.1.27 l-lactate: NAD oxidoreductase, 1.1.1.30 d-3-hydroxybutyrate: NAD oxidoreductase, 1.1.1.37 l-malate: NAD oxidoreductase, 1.1.1.41 threo-ds-isocitrate: NAD oxidoreductase (decarboxylating), 1.1.1.42 threo-ds-isocitrate: NADP oxidoreductase (decarboxylating), 1.1.1.49 d-glucose-6-phosphate: NADP oxidoreductase, 1.1.99.5 l-glycerol-3-phosphate: (acceptor) oxidoreductase, 1.3.99.1 succinate: (acceptor) oxidoreductase, 1.4.1.2 l-glutamate: NAD oxidoreductase (deaminating), 1.6.99.1 reduced-NADP: (acceptor) oxidoreductase, 1.6.99.3 reduced-NAD: (acceptor) oxidoreductase. With the exception of 1.1.1.30 d-3-hydroxybutyrate: NAD oxidoreductase, activity was found throughout the adenohypophysis for all these enzymes. A comparison was made with the activity for these enzymes in liver. In the adenohypophysis, the pars tuberalis exhibited the highest activity for all enzymes, generally equal to or greater than that shown by the liver. The pars intermedia and the pars anterior showed similar activity for these enzymes, in general of a lower order than that given by the liver. The pattern of enzyme distribution in the pars intermedia is described; high activity for 1.1.1.37 l-malate: NAD oxidoreductase, 1.1.1.27 l-lactate: NAD oxidoreductase, 1.6.99.3 reduced-NAD: (acceptor) oxidoreductase, 1.6.99.1 reduced-NADP: (acceptor) oxidoreductase was shown by cells lining cysts and the pituitary cleft. The findings are discussed in relation to the possible association of these enzymes with secretory function.
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