[Hydrophobic nucleus in the primary structure of bovine prolactin].
In the primary structure of bovine prolactin a hydrophobic fragment 79-88 of the peptide chain was found, which participated in a maintenance of conformation of the hormone molecule in a solution due to hydrophobic interactions. The fragment contained about 50% of leucine residues, which are currently considered as important in determination of three-dimensional structure and biological functions of protein (6).
D000085:Acetates; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000440:Butanols; D002417:Cattle; D002854:Chromatography, Paper; D006868:Hydrolysis; D008968:Molecular Conformation; D010446:Peptide Fragments / Q000032:analysis*; D011388:Prolactin / Q000032:analysis*; D014357:Trypsin; D014867:Water
D000085:Acetates; D000596:Amino Acids; D000440:Butanols; D010446:Peptide Fragments; D014867:Water; D011388:Prolactin; D014357:Trypsin
Gidrofobnoe iadro v pervichnoĭ strukture prolaktina krupnogo rogatogo skota