Partial purification of prolactin-like substance from snake (Ptyas mucosa) pituitaries.
Pituitary extract of the common rat snake (Ptyas mucosa) was found to be capable of displacing the binding of 125I-labelled ovine prolactin to female rat liver membranes, suggesting the presence of prolactin-like substance in snake pituitary. The snake prolactin-like substance was unadsorbed on Concanavalin A-Sepharose, but adsorbed on DEAE-cellulose. The partially purified snake prolactin-like substance was also capable of displacing the binding of 125I-labelled ovine prolactin to snake kidney and large intestine membranes. Chromatographic fractions derived from snake pituitary and which possessed potent growth hormone receptor binding activity were devoid of prolactin receptor binding activity, suggesting the existence of distinct prolactin-like and growth hormone-like substances in snake pituitary.
Ng
T B
TB
Department of Biochemistry, University of Hong Kong, Shatin.
Lee
H M
HM
Cheng
C H
CH
Wong
C C
CC
D000818:Animals; D002853:Chromatography, Liquid; D005260:Female; D007457:Iodine Radioisotopes; D008099:Liver / Q000378:metabolism; D010902:Pituitary Gland / Q000737:chemistry*; D011388:Prolactin / Q000302:isolation & purification*; D011485:Protein Binding; D011869:Radioligand Assay; D051381:Rats; D011919:Rats, Inbred Strains; D012911:Snakes / Q000378:metabolism*
D007457:Iodine Radioisotopes; D011388:Prolactin