Abstract
After several erroneous earlier reports, the primary sequences of a family of related proteins exhibiting growth hormone-releasing factor (GRF) properties were reported (Guillemin et al., 1982; Rivier et al., 1982). The proteins were isolated from two different human pancreatic tumors that produced clinical signs of acromegaly, and these sequences differed only in chain length [37 (Esch et al., 1983), 40 (River et al., 1982; Esch et al, 1983), or 44 (Esch et al., 1983) residues]. Further studies with cloned human cDNA (Gubler et al., 1983; Mayo et al., 1983) or protein isolated from human hypothalami (Bohlen et al., 1983; Ling et al., 1984) suggest that the hypothalamic form of hGRF corresponds to the sequence (most likely the GRF1-44-NH2) isolated from the pancreatic tumors (Guillemin et al., 1982). The shorter sequences may result from proteolysis. More recently, the sequences of GRFs (Fig. 1) were reported from the rat (Spiess et al., 1983) and several domestic species (Brazeau et al., 1984).
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© 1986 Plenum Press, New York
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Nestor, J.J., Ho, T.L., DeLustro, B.M., Schreiber, A.B. (1986). Growth Hormone-Releasing Factor Analogues with Increased Receptor Affinity. In: Moody, T.W. (eds) Neural and Endocrine Peptides and Receptors. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5152-8_11
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DOI: https://doi.org/10.1007/978-1-4684-5152-8_11
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