Tryptic digestion of peptides corresponding to modified fragments of human growth hormone-releasing hormone.

Detection of TRH extended peptides in rat hypothalamus using an antibody raised to pGluHisProGlyLys.

An antibody was raised to the synthetic pentapeptide pGluHisProGlyLys which, in radioimmunoassay (RIA), could detect the pentapeptide at a level of 10 fmole per tube and exhibited less than 0.5 per cent cross reactivity with a series of related peptides. The RIA was used to demonstrate the presence of C-terminally extended forms of thyrotropin releasing hormone (TRH) in rat hypothalamus. After ...

The amino acid sequence of a peptide with growth hormone-releasing activity isolated from porcine hypothalamus.

The amino acid sequence of a decapeptide with growth hormone-releasing activity, isolated from porcine hypothalami has been determined. The Edman dansyl procedure was used on the intact peptide and on fragments isolated from tryptic and papain digests. The sequence found was confirmed by the results of digestion with aminopeptidase M, leucine aminopeptidase, and carboxypeptidase A and B. On the...

Comparison of Expression of Growth Hormone-Releasing Hormone and Its Receptor Splice Variant 1 in Different Stages of Endometriosis

Phosphorylation of human growth hormone by the epidermal growth factor-stimulated tyrosine kinase.

In the present study, we have demonstrated that human growth hormone (hGH) can be phosphorylated by the epidermal growth factor (EGF)-stimulated tyrosine kinase of A431 cell membranes. Phosphotyrosine was the predominant phosphoamino acid released from phosphorylated hGH on partial acid hydrolysis. All five tyrosine-containing tryptic peptides of hGH are also phosphorylated by the EGF-stimulate...

Comparisons between the alpha chain of bovine thyrotropin and the CI chain of luteinizing hormone. Compositions of tryptic peptides, cyanogen bromide fragments, and carbohydrate moieties.

The tryptic peptides of reduced, S-carboxymethyl CI chain of bovine luteinizing hormone have been isolated by gel filtration and electrophoresis or chromatography on paper. The amino acid compositions of all peptides are identical with those of the OL chain of thyroid-stimulating hormone (TSH), whose sequence is described in the preceding communication. Chymotryptic-like cleavages also yielded ...