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; Pli\l=s%v\ka,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)
Summary. Fractions enriched with Sertoli cells (S), germ cells (G), and interstitial cells (I) were ...
In an effort to ascertain whether a lysosomal enzyme, aryl sulphatase (ArSase), might share the same...
All five known secretory cell types of the rat anterior pituitary gland display nu-cleoside diphosph...
AbstractGuinea pig neurohypophysial hormones have been purified by two procedures, one involving mol...
The aminopeptidase activity in the brain which converts vasopressin into centrally active metabolite...
AbstractSecretory vesicles isolated from the neural and intermediate lobes of the bovine pituitary c...
AbstractThis paper presents the results obtained when pig anterior pituitary granule lysates are inc...
A cytochemical procedure is reported for identifying subcellular sites of enzymes hydrolyzing beta-n...
The enzymatic conversion of oxytocin by brain peptidases has been studied. Oxytocin was incubated wi...
The cytochemical distribution and changes of ten oxidative enzyme systems were studied in rat anteri...
The distribution of three proteins discharged by regulated exocytosis--growth hormone (GH), prolacti...
The axonal endoplasmic reticulum (ER) and synaptic-like (micro)vesicles within axon terminals of the...
Association of oxytocin and arginine vasopressin with protein in bovine and rabbit neurohypophysial ...
Arginine vasopressin (AVP) acts in the pituitary gland, in synergy with corticotrophin-releasing fac...
The neuropeptides vasopressin and oxytocin were first characterized as hormones, i. e., signalling m...
Summary. Fractions enriched with Sertoli cells (S), germ cells (G), and interstitial cells (I) were ...
In an effort to ascertain whether a lysosomal enzyme, aryl sulphatase (ArSase), might share the same...
All five known secretory cell types of the rat anterior pituitary gland display nu-cleoside diphosph...
AbstractGuinea pig neurohypophysial hormones have been purified by two procedures, one involving mol...
The aminopeptidase activity in the brain which converts vasopressin into centrally active metabolite...
AbstractSecretory vesicles isolated from the neural and intermediate lobes of the bovine pituitary c...
AbstractThis paper presents the results obtained when pig anterior pituitary granule lysates are inc...
A cytochemical procedure is reported for identifying subcellular sites of enzymes hydrolyzing beta-n...
The enzymatic conversion of oxytocin by brain peptidases has been studied. Oxytocin was incubated wi...
The cytochemical distribution and changes of ten oxidative enzyme systems were studied in rat anteri...
The distribution of three proteins discharged by regulated exocytosis--growth hormone (GH), prolacti...
The axonal endoplasmic reticulum (ER) and synaptic-like (micro)vesicles within axon terminals of the...
Association of oxytocin and arginine vasopressin with protein in bovine and rabbit neurohypophysial ...
Arginine vasopressin (AVP) acts in the pituitary gland, in synergy with corticotrophin-releasing fac...
The neuropeptides vasopressin and oxytocin were first characterized as hormones, i. e., signalling m...
Summary. Fractions enriched with Sertoli cells (S), germ cells (G), and interstitial cells (I) were ...
In an effort to ascertain whether a lysosomal enzyme, aryl sulphatase (ArSase), might share the same...
All five known secretory cell types of the rat anterior pituitary gland display nu-cleoside diphosph...