Purification and characterization of glycosylated and non-glycosylated forms of prolactin from the dromedary (Camelus dromedarius).
1. Camel prolactin (camPRL) was isolated from the insoluble residue left after extraction of the gonadotropins FSH and LH from a single batch of one-humped camels (Camelus dromedarius) pituitaries. 2. Several isoforms of camPRL were isolated and characterized. 3. Glycosylated and non-glycosylated forms of camPRL were separated by affinity chromatography on Con-A Sepharose. 4. The glycosylated form represented more than 20% of total camPRL and was found to be only 10-20% as active as the non-glycosylated form in its ability to bind to rabbit mammary gland PRL receptors and to stimulate the proliferation of Nb2 cells.
Martinat
N
N
Station de Physiologie de la Reproduction, INRA and URA CNRS 1291, Nouzilly, France.
Anouassi
A
A
Huet
J C
JC
Pernollet
J C
JC
Combarnous
Y
Y
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002162:Camelus / Q000378:metabolism*; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D013006:Growth Hormone / Q000302:isolation & purification; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D010902:Pituitary Gland / Q000737:chemistry*; D011388:Prolactin / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
D000596:Amino Acids; D011388:Prolactin; D013006:Growth Hormone