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pubmed-article:10529379pubmed:abstractTextThe sex differentiation in crustaceans is known to be controlled by a peptide hormone called androgenic gland hormone (AGH). AGH was extracted and purified from the androgenic glands (AGs) of the male isopod Armadillidium vulgare by high-performance liquid chromatography. AGH consisted of two peptide chains and their N-terminal amino acid sequences were determined. A cDNA encoding AGH was cloned by PCR and sequenced. The cDNA had an open reading frame of 432 bp, which encoded a preproAGH consisting of a signal peptide (21 residues), B chain (44 residues), C peptide (46 residues), and A chain (29 residues). Through processing, the A and B chains might form a heterodimer interlinked by disulfide bonds. The A chain possessed a putative N-linked glycosylation site. A Northern blot analysis using the cDNA as a probe detected a hybridization signal with 0.8 kb in the RNA preparation only from the AGs.lld:pubmed
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pubmed-article:10529379pubmed:copyrightInfoCopyright 1999 Academic Press.lld:pubmed
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pubmed-article:10529379pubmed:volume264lld:pubmed
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pubmed-article:10529379pubmed:pagination419-23lld:pubmed
pubmed-article:10529379pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:10529379pubmed:year1999lld:pubmed
pubmed-article:10529379pubmed:articleTitleCharacterization and cDNA cloning of androgenic gland hormone of the terrestrial isopod Armadillidium vulgare.lld:pubmed
pubmed-article:10529379pubmed:affiliationGraduate School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo, 113-8657, Japan.lld:pubmed
pubmed-article:10529379pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10529379pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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