Binding sites of human growth hormone and ovine and bovine prolactins in the mammary gland and the liver of lactating dairy cow.
Membrane preparations and Triton X-100 solubilized fractions from the mammary gland and liver of the lactating dairy cow were capable of specific binding of [125I]hGH and [125I]oPRL. The specific binding of the latter was significantly lower and could not be increased by higher receptor levels. Displacement studies of [125I]hGh by hGH, bPRL and oPRL revealed that the two latter hormones have a 20-40-fold lower affinity for the receptor than hGH, although strong indications exist that they all bind or the same sites. This feature is unique for cows and does not exist or is much less pronounced in rodents.
D000818:Animals; D002417:Cattle; D005260:Female; D013006:Growth Hormone / Q000378:metabolism*; D007700:Kinetics; D007774:Lactation; D008099:Liver / Q000378:metabolism*; D008321:Mammary Glands, Animal / Q000378:metabolism*; D011247:Pregnancy; D011388:Prolactin / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism; D011981:Receptors, Prolactin; D011986:Receptors, Somatotropin; D012756:Sheep
D011956:Receptors, Cell Surface; D011981:Receptors, Prolactin; D011986:Receptors, Somatotropin; D011388:Prolactin; D013006:Growth Hormone