The precursors of peptide hormones that possess a COOH-terminal alpha-amide group contain a glycine residue following the amino acid which is amidated in the hormone. Less than Glu-His-Pro-Gly was synthesized as a putative precursor of thyroliberin. Bovine pituitary neurosecretory granules were shown to contain an amide group-forming activity associated with an Mr of about 62 000 protein(s) which converts the tetrapeptide to thyroliberin.
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Husain et al. (1983) studied this question.
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