[Degradation of 125I-prolactin in the mammae and kidneys of lactating rats].
The degradation of sheep and rat 125I-prolactin was studied. It was shown that in the breast tissues, there were specific prolactin degrading proteases. The maximal activity of breast proteases was noted at pH 7.6 and 3.0. Neutral proteases were located in the nucleic and mitochondrial fractions, acid proteases mostly in the lysosomal fraction. Some data indicating the participation of the receptors of the breast sensitive nerves in the regulation of prolactin degrading neutral protease activity were obtained. Apart from degradation products from the breast and kidneys, a high molecular complex was extracted. After treatment with mercaptoethanol it dissociated with the release of a 125I-prolactin monomer. It is assumed that high-molecular products extracted from the tissues are a soluble hormone-receptor complex.
D000818:Animals; D005260:Female; D007668:Kidney / Q000201:enzymology*; D007774:Lactation; D008321:Mammary Glands, Animal / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011247:Pregnancy; D011388:Prolactin / Q000008:administration & dosage; D051381:Rats; D011919:Rats, Inbred Strains; D012756:Sheep
D011388:Prolactin; D010447:Peptide Hydrolases
Degradatsiia 125I-prolaktina v molochnoĭ zheleze i pochkakh laktiruiushchikh krys.