In earlier studies it was shown that oxytocin and vasopressin were broken down by peptidases present in the neurohypophyses of the rat, pig and ox (Edwards, 1971a, b; Pliška, Thorn & Vilhardt, 1971). The present work was carried out to determine the subcellular localization of this enzymic activity with special interest in the lysosomes whose function as a mechanism of controlling excess hormone in the anterior pituitary has been suggested by Smith & Farquhar (1966).
Separation of the various subcellular fractions was carried out using a differential centrifugation procedure suggested by A. Livingston (personal communication). Four fractions were prepared: A (1000 g for 10 min), B (5000 g for 10 min), C (25 000 g for 20 min) and D (the final supernatant). Each fraction was analysed for vasopressin (hormonal marker), cathepsin (lysosomal marker), fumarase (mitochondrial marker) and lactate dehydrogenase (cytoplasmic marker). Complete separation into discrete fractions was not
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