Alteration of human placental lactogen by mammary gland.

Human placental lactogen was prepared in high purity and in good yield applying a minimum of purification steps. The isolated hormone was characterized with respect to isoelectric and electrophoretic properties, molecular size (estimated mol. wt. 23 000) and stability to heat, pH and organic solvents. Investigation of in vitro interaction between placental lactogen and mammary gland (mouse, rat) revealed a rapid alteration of hormone with loss of immunoreactivity resulting. The target organ as a selective alteration site of placental lactogen was suggested by a lack of similar action on the hormone by a number of other tissues tested, including liver, kidney and lung. The reaction involving hormone alteration by mammary gland was localized to a particulate-bound enzyme, sedimentable at 10 000 X g and undissociated by sonication in 0.5% Triton X-100. Examination of the reaction products revealed hormone degradation with formation of diffusible components and loss of original electrophoretic identity as well as immunoreactive properties. The reaction characteristics included: pH optimum between 7.5 and 8.0, an absolute salt requirement (NaCl, KCl, at concentration greater than 0.15 M for maximal activation), inhibition by Cleland's reagent and lack of reaction interference by pituitary prolactin.