Open AccessHuman somatotropin: covalent reconstitution of two polypeptide contiguous fragments with thrombin.
Author(s) -
László Gráf,
C H Li
Publication year - 1981
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.78.10.6135
Subject(s) - thrombin , radioimmunoassay , sodium dodecyl sulfate , chemistry , peptide , gel electrophoresis , glycerol , covalent bond , biochemistry , chromatography , medicine , platelet , organic chemistry
Thrombin has been shown to resynthesize the Arg134-Thr135 peptide bond between the 134- and 57-residue thrombin fragments of reduced and carbamidomethylated human somatotropin at pH 6.0 in 90% (vol/vol) glycerol. The maximal amount of synthesis was about 20% as estimated by sodium dodecyl sulfate gel electrophoresis and radioreceptor assay. The resynthesized polypeptide was isolated and shown to be indistinguishable from the reduced and carbamidomethylated hormone when tested by two receptor-binding assays, radioimmunoassay, and rat tibia test.