title: Purification and partial characterization of growth hormone from the dromedary (Camelus dromedarius).
abstract: Camel growth hormone (camGH) was isolated from the insoluble residue left after extraction of the gonadotropins FSH and LH from a single batch of one-humped camel (Camelus dromedarius) pituitaries. Only one form of camGH was isolated and characterized; no glycosylated form of camGH could be evidenced. The isoelectric points (pI) of camGH was determined by chromatofocusing. The N-terminal amino-acid sequences of camGH was determined and compared to those of GHs from other species. The availability of this hormone and our better knowledge of its structure will permit to undertake the study of its structure-function relationships and of its physiological functions in this economically important species.
authors: Institut National de la Recherche Agronomique & URA CNRS 1291, Station de Physiologie de la Reproduction, Nouzilly, France.
authors: N
authors: N
authors: Martinat
authors: A
authors: A
authors: Anouassi
authors: J C
authors: JC
authors: Huet
authors: J C
authors: JC
authors: Pernollet
authors: V
authors: V
authors: Segard
authors: Y
authors: Y
authors: Combarnous
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002162:Camelus / Q000378:metabolism*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D013006:Growth Hormone / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011110:Polymorphism, Genetic; D011487:Protein Conformation; D011863:Radioimmunoassay; D011869:Radioligand Assay
chemical_list: D000596:Amino Acids; D013006:Growth Hormone