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A 44 amino acid peptide with high intrinsic growth hormone releasing activity was isolated from 2500 porcine hypothalami by means of acid extraction, immunoaffinity chromatography, gel filtration, and 2 steps of reverse phase HPLC. The growth hormone releasing factor was structurally characterized by gas phase sequence analyses of the intact peptide and its carboxyl terminal cyanogen bromide digestion fragment. Reverse phase liquid chromatography of the native peptide and synthetic replicates showed that the molecule possesses an amide rather than a free acid at its carboxyl terminus. The structure of the peptide was established as: Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Arg-Asn-Gln-Glu-Gln-Gly-Ala-Arg-Val-Arg-Leu-NH2 using approximately 6 nmol of material.
P Böhlen, and
F Esch, and
P Brazeau, and
N Ling, and
R Guillemin
January 1983,
Nature,
P Böhlen, and
F Esch, and
P Brazeau, and
N Ling, and
R Guillemin
October 1992,
Neuroendocrinology,
P Böhlen, and
F Esch, and
P Brazeau, and
N Ling, and
R Guillemin
August 1982,
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P Böhlen, and
F Esch, and
P Brazeau, and
N Ling, and
R Guillemin
December 1970,
Nihon Naibunpi Gakkai zasshi,
P Böhlen, and
F Esch, and
P Brazeau, and
N Ling, and
R Guillemin
December 1984,
The Journal of experimental zoology,
P Böhlen, and
F Esch, and
P Brazeau, and
N Ling, and
R Guillemin
June 1969,
Endocrinology,
P Böhlen, and
F Esch, and
P Brazeau, and
N Ling, and
R Guillemin
August 1984,
Biochemical and biophysical research communications,
P Böhlen, and
F Esch, and
P Brazeau, and
N Ling, and
R Guillemin
September 1982,
The Journal of biological chemistry,
P Böhlen, and
F Esch, and
P Brazeau, and
N Ling, and
R Guillemin
January 1987,
Gene,
P Böhlen, and
F Esch, and
P Brazeau, and
N Ling, and
R Guillemin
April 1986,
Chemical & pharmaceutical bulletin,
