Open AccessCloning and sequence analysis of cDNA for the precursor of human growth hormone-releasing factor, somatocrinin.
Author(s) -
Ueli Gubler,
John J. Monahan,
Peter T. Lomedico,
Rachana Bhatt,
Kenneth J. Collier,
Beth J. Hoffman,
Peter Böhlen,
Frederick Esch,
Nicholas Ling,
Füsûn N. Zeytin,
Paul Brazeau,
Mohindar S. Poonian,
L. Patrick Gage
Publication year - 1983
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.80.14.4311
Subject(s) - complementary dna , immunoprecipitation , biology , microbiology and biotechnology , molecular cloning , serine , signal peptide , messenger rna , cloning (programming) , antiserum , peptide sequence , sequence (biology) , gel electrophoresis , biochemistry , gene , genetics , antibody , enzyme , computer science , programming language
Molecular cloning has established the primary structures of two precursors of the human pancreas growth hormone-releasing factor (hpGRF-44), somatocrinin. Both polypeptides contain the sequence of hpGRF-44 flanked by basic processing sites. Furthermore, the precursors include a putative signal sequence and a carboxyl-terminal amidation signal for hpGRF-44. The two forms of mRNA code for pre-pro-GRF-107 and pre-pro-GRF-108. Pre-pro-GRF-108 differs from pre-pro-GRF-107 by the insertion of a serine in the carboxyl-terminal portion of the precursor. In vitro translation of tumor poly(A)+ RNA followed by immunoprecipitation with GRF-specific antiserum and gel electrophoresis showed the molecular weight of preprosomatocrinin to be approximately 13,000, which is in good agreement with the molecular weight deduced from the sequences of the cDNA clones.