POTENCIES OF PORCINE RELAXINS USING TWO BIOASSAYS

in Journal of Endocrinology
Authors:
W. A. CHAMLEY
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MARLENE M. BAGOYO
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GILLIAN D. BRYANT-GREENWOOD
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Relaxin reference preparations NIH-R-P1 and Warner Lambert W1164-3, and purified relaxin peptides, CM-a′, CM-a and CM-B, were assayed in the mouse interpubic ligament and rat uterine inhibition bioassays. There was evidence that CM-a and CM-B would bind to glass and significant apparent increases in potency in the case of these two peptides alone resulted from the use of silicone-coated glassware. Using treated glassware, CM-a′, CM-a and CM-B were equipotent in the mouse interpubic ligament bioassay with potencies relative to NIH-R-P1 of 3·97-, 4·85- and 3·64-fold respectively. In the rat uterine inhibition bioassay only W1164-3 and CM-a′ gave dose-response curves which were parallel to NIH-R-P1. In this bioassay, potencies relative to NIH-R-P1 for W1164-3 and CM-a' were 0·35-and 19·6-fold respectively.

 

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