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16 recordsLinked to original sources
PubMed1962

Effect of tyrosinase preparations on oxytocin, vasopressin and bradykinin.

On incubation with a tyrosinase preparation at pH 7.5, oxytocin and vasopressin were inactivated. The loss of oxytocic activity did not differ significantly from that of milk-ejecting activity in oxytocin, nor the loss of pressor activity from that of antidiuretic activity in vasopressin. Oxytocin was inactivated less rapidly at pH 6.6 than at pH 7.5. At pH 3.9 neither oxytocin nor vasopressin was inactivated. Analogues of oxytocin and vasopressin, in which tyrosine is replaced by phenylalanine, were not inactivated by the tyrosinase preparation used. On incubation of bradykinin with two different tyrosinase preparations, there was no loss of oxytocic activity at pH 7.5 but an almost total loss at pH 3.9. In the presence of p-nitrophenol, ascorbic acid, sodium diethyldithiocarbamate and during incubation under anaerobic conditions the inactivation of oxytocin at pH 7.5 was inhibited, but not that of bradykinin at pH 3.9. It is concluded that the tyrosinase preparations used contain two distinct enzymes or activities, the one inactivating oxytocin and vasopressin at pH 7.5 and the other bradykinin at pH 3.9.

Arginine Vasopressin↗
PubMed1962

Assay of oxytocin by rat mammary gland in vitro.

A new method for quantitative assay of oxytocin using strips from rat mammary gland in vitro has been investigated. The method is very suitable for determination of small amounts of oxytocin. Doses down to 2 mu-u. oxytocin have been estimated. The dose-response curve is shown to be linear, and the precision of the method is good (lambda =0.10 to 0.14). The effect of adrenaline, noradrenaline, acetylcholine, histamine and 5-hydroxytryptamine on the rat mammary gland has also been tested.

Acetylcholine↗