Isoforms of turkey prolactin: evidence for differences in glycosylation and in tryptic peptide mapping.
1. Three isoforms of turkey pituitary prolactin have been isolated, including a nonglycosylated isoform of 22,500 mol. wt and two glycosylated isoforms of 24,500 mol. wt. 2. The glycosylated turkey prolactins differed in carbohydrate composition, with one isoform apparently containing only O-linked carbohydrate. 3. Tryptic peptide maps showed a few peptides distinctly different among the three prolactin isoforms. 4. Amino acid sequencing of the first 40 residues of the three prolactin isoforms showed arginine at position 24 and histidine at position 27, for the nonglycosylated form, but no identifiable amino acids were detected at this position for the glycosylated isoforms.
Corcoran
D H
DH
Department of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, MD 20814.
Proudman
J A
JA
D000595:Amino Acid Sequence; D000818:Animals; D005260:Female; D006031:Glycosylation; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010449:Peptide Mapping; D010902:Pituitary Gland / Q000737:chemistry; D011388:Prolactin / Q000737:chemistry / Q000302:isolation & purification*; D011869:Radioligand Assay; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D014357:Trypsin; D014422:Turkeys / Q000378:metabolism*
D011388:Prolactin; D014357:Trypsin