title: Changes of lactic dehydrogenase activity and combination of its subunits in rat anterior pituitary during puberty and in maturity, as well as during estrous cycle on the actue effect of estradiol and after castration.
abstract: LDH activity in the female rat anterior pituitary increases substantially at the opening of the vagina, after the gradual increase up to the 90st day no important change occurs. During the estrous cycle activity reaches its peak during the estrus, and lowest in ghe proestrus. Molecular organization of the enzyme shows a change only at the opening of the vagina, i. e. a sudden decrease of H/M ratio occurs, value of which does not change during the estrous cycle. Pituitary LDH activity and subunit ratio in males remains constant during life. LDH activity excess in mature female rat pituitary, being about the double as compared to males, develops at the age of about three months, the difference in H/M ratio however is manifest already during puberty. Anterior pituitary LDH activity and structure of the enzyme are affected by sexual hormones, primarily by estradiol, under physiological conditions, too. After ovariectomy LDH activity decreases gradually. The value before the opening of the vagina to be considered as basal level, develops in the 4th postoperative week. H/M  ratio decreases by 20 per cent one week after the operation and shows no change thereafter. Orchidectomy involves but a minor activity and H/M ratio decrease. Experimental findings on activity and subunit ratio are related presumably to prolactin cells and suggest that sexual hormone feedback effects in addition to polypeptide production pituitary metabolism.
mesh_terms: D000818:Animals; D002369:Castration; D004958:Estradiol / Q000502:physiology; D004971:Estrus; D005260:Female; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D008297:Male; D010903:Pituitary Gland, Anterior / Q000378:metabolism*; D011247:Pregnancy; D051381:Rats; D012741:Sexual Maturation
chemical_list: D004958:Estradiol; D007770:L-Lactate Dehydrogenase