Copurification of prostaglandin F2 alpha receptors with rat uterine plasma membranes.
Myometrial homogenates of estrogen-treated nonpregnant rats were fractionated by differential and discontinuous sucrose gradient centrifugation. Binding of PGF2 alpha was maximal in membrane fraction which showed the highest specific activity of 5'-nucleotidase, a marker for plasma membrane.
D015720:5'-Nucleotidase; D000818:Animals; D002458:Cell Fractionation; D002462:Cell Membrane / Q000032:analysis; D015237:Dinoprost; D005260:Female; D009708:Nucleotidases / Q000032:analysis; D011460:Prostaglandins F / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D011956:Receptors, Cell Surface / Q000302:isolation & purification*; D011982:Receptors, Prostaglandin / Q000302:isolation & purification*; D014599:Uterus / Q000648:ultrastructure*
D011460:Prostaglandins F; D011956:Receptors, Cell Surface; D011982:Receptors, Prostaglandin; C034671:prostaglandin F2alpha receptor; D015237:Dinoprost; D009708:Nucleotidases; D015720:5'-Nucleotidase