Human urinary insulin-potentiating peptide: immunological evidence for the absence of the human growth hormone amino terminal sequence, Phe-Pro-Thr-Ile-Pro-.
The immunological reactivities of synthetic partial sequences of human growth hormone (hGH) and of an insulin-potentiating peptide isolated from human urine were studied using an antiserum raised against a synthetic hGH analogue [beta-Ala13]hGH(1-15). This antiserum contained antibodies directed mainly against a determinant in the sequence hGH(1-5). It was found that synthetic peptides containing the sequence Phe-Pro-Thr-Ile-Pro- (residues 1-5 of hGH) were immunologically active. Of the biologically active peptides studied, the synthetic peptide hGH(6-13) was virtually inactive and the urinary peptide was completely inert. Absence of immunologically detectable cross-reactivity lends support to the hypothesis that the amino acid sequence of urinary insulin-potentiating peptide (U-AcG) does not contain the hGH amino terminal sequence, Phe-Pro-Thr-Ile-Pro-.
D000595:Amino Acid Sequence; D000818:Animals; D000918:Antibody Specificity; D013006:Growth Hormone / Q000276:immunology / Q000652:urine*; D006801:Humans; D007120:Immunochemistry; D010446:Peptide Fragments / Q000276:immunology / Q000652:urine*; D051381:Rats
D010446:Peptide Fragments; C023716:acceleratory factor from growth hormone; D013006:Growth Hormone