Recombination of the biologically active peptides from a tryptic digest of bovine growth hormone

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Abstract
Two bovine growth hormone peptides containing residues 96-133 in one and a larger peptide corresponding to residues 1-95 and 151-191 linked by a disulfide bond were recombined. Recombination was performed in 1.0 N acetic acid without and with 8 M urea and the recombined peptides were purified by gel filtration. Evidence of recombination of the peptides was established by gel filtration, polyacrylamide gel disc electrophoresis, amino acid composition, UV absorption, circular dichroism and intrinsic fluorescence. The molar growth promoting activity of the recombined peptides measured by tibial width assay in hypophysectomized rats was 10% that of the native hormone and greater than the sum (1%) of the growth promoting activities of the individual peptides. Some contribution of the larger peptide may be necessary for more complete expression of the growth promoting activity of the bovine growth peptide corresponding to residues 96-133.