Isolation and characterisation of a novel peptide from ostrich adenohypophyses.
A novel peptide has been isolated from ostrich pituitary glands using acid acetone extraction, salt fractionation, ion exchange and gel permeation chromatography and preparative paper electrophoresis. The homogeneous fraction contained a large proportion of hydrophobic amino acids apparently concentrated in a portion of the polypeptide. An amino-terminal isoleucine and carboxyl-terminal glutamine were found. The molecular weight was determined as 15 024 (ultracentrifugation) and 16 185 (amino acid analysis). A single intra-molecular disulfide bond was determined. The isoelectric point was 6.5. A possible role as part of a hormone precursor is suggested.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001717:Birds / Q000502:physiology*; D002850:Chromatography, Gel; D003488:Cyanogen Bromide; D004220:Disulfides / Q000032:analysis; D008970:Molecular Weight; D010455:Peptides / Q000302:isolation & purification*; D010903:Pituitary Gland, Anterior / Q000032:analysis*
D000596:Amino Acids; D004220:Disulfides; D010455:Peptides; D003488:Cyanogen Bromide