3H]tyrosine binding to plasma membrane preparation of rat corpora lutea.

Abstract

Plasma membrane preparations of rat corpora lutea have been incubated with [3H]tyrosine. [3H]tyrosine binding sites are demonstrated and Scatchard analysis shows that there exist two types of binding sites, one with high affinity and low capacity, the other with low affinity and high capacity. The kinetics studies demonstrate that the [3H]tyrosine binding to the two types of binding sites is reversible and the speed of binding to the high affinity type is faster than that to the low affinity type. The analysis of the chemical structure of tyrosine analogues and related compounds with respect to the specificity of the binding sites reveal that both types of binding sites show specificity, but the specificity of the high affinity sites is higher than that of the low affinity sites. The relations of tyrosine structure to binding processing and to tyrosine inhibitory action on hCG-induced progesterone production are discussed. It is suggested that the high affinity binding sites might be regarded as "tyrosine receptors" and the low affinity ones glycoprotein carriers for tyrosine across the plasma membrane.