Sialic acid moiety is responsible for the charge heterogeneity and the biological potency of rat lutropin.
To elucidate a possible role of sialic acid moiety in the electrical heterogeneity of rat pituitary lutropin, seven components separated were individually treated with neuraminidase. Some intermediates with isoelectric points corresponding to the native components were concomitantly seen at the serial stages of the enzyme treatment. All the treated components showed an isoelectric point of about 10.0 which was the same to the isoelectric point of one of the seven components. Desialylation of the components with less biological activity caused enhancement of the in vitro cyclic AMP producing- and testosterone producing-activities as well as the binding activity to the receptor. It is concluded that the number of sialic acid moiety in lutropin is responsible for the charge heterogeneity and the biological potency of the hormone.
Hattori
M
M
Ozawa
K
K
Wakabayashi
K
K
D000818:Animals; D001667:Binding, Competitive; D055598:Chemical Phenomena; D002621:Chemistry; D006063:Chorionic Gonadotropin / Q000378:metabolism; D066298:In Vitro Techniques; D007525:Isoelectric Focusing; D007985:Leydig Cells / Q000378:metabolism; D007986:Luteinizing Hormone / Q000032:analysis* / Q000502:physiology; D008297:Male; D019158:N-Acetylneuraminic Acid; D009439:Neuraminidase; D010902:Pituitary Gland / Q000032:analysis; D051381:Rats; D011956:Receptors, Cell Surface / Q000378:metabolism; D011974:Receptors, LH; D012794:Sialic Acids / Q000032:analysis*
D006063:Chorionic Gonadotropin; D011956:Receptors, Cell Surface; D011974:Receptors, LH; D012794:Sialic Acids; D007986:Luteinizing Hormone; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid