Abstract:
:Pancreatic polypeptide (PP) has been isolated from pancreatic extracts of the herring gull (Larus argentatus) using a radioimmunoassay employing an antiserum (PP 221), generated to the conserved C-terminal hexapeptide amide of mammalian PP. Gel permeation and reverse-phase HPLC fractionation of crude pancreatic extracts resolved a single molecular form of gull PP in each case. Purification of gull PP to homogeneity indicated that the mammalian PP antiserum employed was only 4% cross-reactive with this peptide. When radioimmunoassay data were corrected for this, the herring gull pancreas was found to contain 5 nmol PP/g wet wt. The molecular mass of gull PP was determined as 4237 +/- 2 Da by 252Cf plasma desorption mass spectroscopy (PDMS). Gas-phase sequencing established unequivocally the entire primary structure of a 36-amino-acid residue peptide as Gly-Pro-Val-Gln-Pro-Thr-Tyr-Pro-Gly-Asp-Asp-Ala-Pro-Val-Glu-Asp-Leu-Val- Arg-Phe - Try-Asn-Asp-Leu-Gln-Gln-Tyr-Leu-Asn-Val-Val-Thr-Arg-His-Arg-Tyr. The computed molecular mass of this peptide (4235.6 Da) was in close agreement with that derived by PDMS. The primary structure of herring gull PP differs from that of the chicken in four residues at positions 3 (Val/Ser), 18 (Val/IIe), 22 (Asn/Asp), and 23 (Asp/Asn). Avian PP thus appears to be a highly conserved regulatory peptide.
journal_name
Gen Comp Endocrinoljournal_title
General and comparative endocrinologyauthors
Barton CL,Shaw C,Halton DW,Thim Ldoi
10.1006/gcen.1994.1029subject
Has Abstractpub_date
1994-02-01 00:00:00pages
255-9issue
2eissn
0016-6480issn
1095-6840pii
S0016-6480(84)71029-Xjournal_volume
93pub_type
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