Amino-acid Sequence of a Melanophore-stimulating Peptide
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چکیده
منابع مشابه
Regulation of melanophore stimulating hormone (MSH) release.
Melanin pigmentation of the vertebrate integument is regulated by melanophore-stimulating hormone (MSH) which originates from the pars intermedia of the pituitary gland (1). Early experiments established that MSH release, as for other pituitary secretions, was under control by the hypothalamus (2). Similar to prolactin release (3), MSH secretion is under an inhibitory control by the hypothalamu...
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The amino acid sequence of neuropeptide Y, a 36-residue peptide recently isolated from porcine brain, has been determined by using high performance liquid chromatography for separation of its tryptic and chymotryptic fragments and subsequent sequence analysis of the isolated fragments by an improved dansyl Edman subtractive technique. The amino acid sequence of neuropeptide Y has been found to ...
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Background and Aims: Since 1998, Iranian poultry industry has been affected by avian influenza (AI) virus, subtype H9N2. The association of high mortality and case report of H5N1 and H9N2 influenza virus in wild birds in recent years raised the suspicion of a possible new genetic modified AI virus. Methods: Partial nucleotide sequences and deduced amino acid of hemagglutinin (HA) genes of 4 H9...
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The beta subunit of follicle-stimulating hormone (FSH-beta) from human pituitary glands was reduced and S-aminoethylated prior to thermolytic, tryptic, and chymotryptic digestions. Each digest was gel-filtered on Sephadex G-50 to seperate the glycopeptides. The glycopeptides and the peptides were isolated by high voltage paper electrophoresis at pH 6, 3.5, and 2.0. The purity of the isolated pe...
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The p subunit of follicle-stimulating hormone (FSH-@) from human pituitary glands was reduced and S-aminoethylated prior to thermolytic, tryptic, and chymotryptic digestions. Each digest was gel-filtered on Sephadex G-50 to separate the glycopeptides from the peptides. The glycopeptides and the peptides were isolated by high voltage paper electrophoresis at pH 6, 3.5, and 2.0. The purity of the...
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ژورنال
عنوان ژورنال: Nature
سال: 1956
ISSN: 0028-0836,1476-4687
DOI: 10.1038/178090a0