Cloning, expression, and biological activity of growth hormone in bullfrog ( Rana catesbeiana)
The cDNA (GenBank, AY251538) encoding bullfrog growth hormone (fGH) was cloned by RT-PCR from the total RNA of pituitary glands. Its sequence encoded a putative polypeptide of 215 amino acids, including a signal peptide of 25 amino acids with no change to those of other previous reported bullfrog GH...
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Veröffentlicht in: | General and comparative endocrinology 2006-05, Vol.146 (3), p.296-303 |
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description | The cDNA (GenBank, AY251538) encoding bullfrog growth hormone (fGH) was cloned by RT-PCR from the total RNA of pituitary glands. Its sequence encoded a putative polypeptide of 215 amino acids, including a signal peptide of 25 amino acids with no change to those of other previous reported bullfrog GHs. The
fGH precursor shares 98.1, 96.3, and 95.3% homologies to those of other bullfrog GHs (AAB24792, AAB19428, CAA31038) in amino-acid sequence and its nucleotide sequences of the coding region shares 99.1 and 98.5% homologies to those of previous bullfrog GH genes (S52027 and X12520). The fGH cDNA was also efficiently expressed in
Escherichia coli carrying a plasmid pGfGH in which the cDNA was under the control of GST promoter of pGEX1-λT. The expressed fusion protein
GST-fGH is comprised about 29.3% of the total cellular protein in such bacteria. The purified
GST-fGH cannot only showed a obvious dose–response curve when it reacted with the hepatic membrane receptor proteins from bullfrog, but also significantly increased the body weight and length of bullfrog after twice injection and such effects lasted two or three weeks after the last injection with purified
GST-fGH. |
doi_str_mv | 10.1016/j.ygcen.2005.11.017 |
format | Article |
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fGH precursor shares 98.1, 96.3, and 95.3% homologies to those of other bullfrog GHs (AAB24792, AAB19428, CAA31038) in amino-acid sequence and its nucleotide sequences of the coding region shares 99.1 and 98.5% homologies to those of previous bullfrog GH genes (S52027 and X12520). The fGH cDNA was also efficiently expressed in
Escherichia coli carrying a plasmid pGfGH in which the cDNA was under the control of GST promoter of pGEX1-λT. The expressed fusion protein
GST-fGH is comprised about 29.3% of the total cellular protein in such bacteria. The purified
GST-fGH cannot only showed a obvious dose–response curve when it reacted with the hepatic membrane receptor proteins from bullfrog, but also significantly increased the body weight and length of bullfrog after twice injection and such effects lasted two or three weeks after the last injection with purified
GST-fGH.</description><identifier>ISSN: 0016-6480</identifier><identifier>EISSN: 1095-6840</identifier><identifier>DOI: 10.1016/j.ygcen.2005.11.017</identifier><identifier>PMID: 16442533</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Biological activity ; Bullfrog growth hormone ; cDNA cloning ; Cloning, Molecular ; Escherichia coli ; Expression ; Glutathione Transferase - genetics ; Growth Hormone - genetics ; Growth Hormone - pharmacology ; Molecular Sequence Data ; Rana catesbeiana ; Rana catesbeiana - growth & development ; Recombinant Fusion Proteins - metabolism ; Sequence Alignment</subject><ispartof>General and comparative endocrinology, 2006-05, Vol.146 (3), p.296-303</ispartof><rights>2005 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c388t-7a641712a91cb2832446f1a10044a2641b29eae0f441dd9151ac546c23c7cee43</citedby><cites>FETCH-LOGICAL-c388t-7a641712a91cb2832446f1a10044a2641b29eae0f441dd9151ac546c23c7cee43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0016648005003473$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16442533$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yu, Lin</creatorcontrib><creatorcontrib>Chen, Xiaomei</creatorcontrib><creatorcontrib>Liu, Shigui</creatorcontrib><creatorcontrib>Long, Zhangfu</creatorcontrib><title>Cloning, expression, and biological activity of growth hormone in bullfrog ( Rana catesbeiana)</title><title>General and comparative endocrinology</title><addtitle>Gen Comp Endocrinol</addtitle><description>The cDNA (GenBank, AY251538) encoding bullfrog growth hormone (fGH) was cloned by RT-PCR from the total RNA of pituitary glands. Its sequence encoded a putative polypeptide of 215 amino acids, including a signal peptide of 25 amino acids with no change to those of other previous reported bullfrog GHs. The
fGH precursor shares 98.1, 96.3, and 95.3% homologies to those of other bullfrog GHs (AAB24792, AAB19428, CAA31038) in amino-acid sequence and its nucleotide sequences of the coding region shares 99.1 and 98.5% homologies to those of previous bullfrog GH genes (S52027 and X12520). The fGH cDNA was also efficiently expressed in
Escherichia coli carrying a plasmid pGfGH in which the cDNA was under the control of GST promoter of pGEX1-λT. The expressed fusion protein
GST-fGH is comprised about 29.3% of the total cellular protein in such bacteria. The purified
GST-fGH cannot only showed a obvious dose–response curve when it reacted with the hepatic membrane receptor proteins from bullfrog, but also significantly increased the body weight and length of bullfrog after twice injection and such effects lasted two or three weeks after the last injection with purified
GST-fGH.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biological activity</subject><subject>Bullfrog growth hormone</subject><subject>cDNA cloning</subject><subject>Cloning, Molecular</subject><subject>Escherichia coli</subject><subject>Expression</subject><subject>Glutathione Transferase - genetics</subject><subject>Growth Hormone - genetics</subject><subject>Growth Hormone - pharmacology</subject><subject>Molecular Sequence Data</subject><subject>Rana catesbeiana</subject><subject>Rana catesbeiana - growth & development</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sequence Alignment</subject><issn>0016-6480</issn><issn>1095-6840</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFq3DAQhkVpaDZJn6BQdCoJrF2NLMv2IYewNE0gEAjNtUKWx44Wr7SVvGn37aPNLvSWnGZgvv8f-Aj5AiwHBvL7Mt8OBl3OGStzgJxB9YHMgDVlJmvBPpIZS1gmRc2OyUmMS5bAQsIncgxSCF4WxYz8XozeWTfMKf5bB4zRejen2nW0tX70gzV6pNpM9tlOW-p7OgT_d3qiTz6svENqHW0349gHP9Bz-qCdpkZPGFu0ab84I0e9HiN-PsxT8nj949fiJru7_3m7uLrLTFHXU1ZpKaACrhswLa8LLoTsQQNjQmiebi1vUCPrhYCua6AEbUohDS9MZRBFcUq-7XvXwf_ZYJzUykaD46gd-k1UsqrrksvmXRCaSjZlVSew2IMm-BgD9mod7EqHrQKmdv7VUr36Vzv_CkAl_yn19VC_aVfY_c8chCfgcg9gsvFsMahoLDqDnQ1oJtV5--aDFwM2ls0</recordid><startdate>20060501</startdate><enddate>20060501</enddate><creator>Yu, Lin</creator><creator>Chen, Xiaomei</creator><creator>Liu, Shigui</creator><creator>Long, Zhangfu</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7TK</scope><scope>C1K</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>20060501</creationdate><title>Cloning, expression, and biological activity of growth hormone in bullfrog ( Rana catesbeiana)</title><author>Yu, Lin ; Chen, Xiaomei ; Liu, Shigui ; Long, Zhangfu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-7a641712a91cb2832446f1a10044a2641b29eae0f441dd9151ac546c23c7cee43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biological activity</topic><topic>Bullfrog growth hormone</topic><topic>cDNA cloning</topic><topic>Cloning, Molecular</topic><topic>Escherichia coli</topic><topic>Expression</topic><topic>Glutathione Transferase - genetics</topic><topic>Growth Hormone - genetics</topic><topic>Growth Hormone - pharmacology</topic><topic>Molecular Sequence Data</topic><topic>Rana catesbeiana</topic><topic>Rana catesbeiana - growth & development</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Sequence Alignment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yu, Lin</creatorcontrib><creatorcontrib>Chen, Xiaomei</creatorcontrib><creatorcontrib>Liu, Shigui</creatorcontrib><creatorcontrib>Long, Zhangfu</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Neurosciences Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>General and comparative endocrinology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yu, Lin</au><au>Chen, Xiaomei</au><au>Liu, Shigui</au><au>Long, Zhangfu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning, expression, and biological activity of growth hormone in bullfrog ( Rana catesbeiana)</atitle><jtitle>General and comparative endocrinology</jtitle><addtitle>Gen Comp Endocrinol</addtitle><date>2006-05-01</date><risdate>2006</risdate><volume>146</volume><issue>3</issue><spage>296</spage><epage>303</epage><pages>296-303</pages><issn>0016-6480</issn><eissn>1095-6840</eissn><abstract>The cDNA (GenBank, AY251538) encoding bullfrog growth hormone (fGH) was cloned by RT-PCR from the total RNA of pituitary glands. Its sequence encoded a putative polypeptide of 215 amino acids, including a signal peptide of 25 amino acids with no change to those of other previous reported bullfrog GHs. The
fGH precursor shares 98.1, 96.3, and 95.3% homologies to those of other bullfrog GHs (AAB24792, AAB19428, CAA31038) in amino-acid sequence and its nucleotide sequences of the coding region shares 99.1 and 98.5% homologies to those of previous bullfrog GH genes (S52027 and X12520). The fGH cDNA was also efficiently expressed in
Escherichia coli carrying a plasmid pGfGH in which the cDNA was under the control of GST promoter of pGEX1-λT. The expressed fusion protein
GST-fGH is comprised about 29.3% of the total cellular protein in such bacteria. The purified
GST-fGH cannot only showed a obvious dose–response curve when it reacted with the hepatic membrane receptor proteins from bullfrog, but also significantly increased the body weight and length of bullfrog after twice injection and such effects lasted two or three weeks after the last injection with purified
GST-fGH.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16442533</pmid><doi>10.1016/j.ygcen.2005.11.017</doi><tpages>8</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Biological activity Bullfrog growth hormone cDNA cloning Cloning, Molecular Escherichia coli Expression Glutathione Transferase - genetics Growth Hormone - genetics Growth Hormone - pharmacology Molecular Sequence Data Rana catesbeiana Rana catesbeiana - growth & development Recombinant Fusion Proteins - metabolism Sequence Alignment |
title | Cloning, expression, and biological activity of growth hormone in bullfrog ( Rana catesbeiana) |
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