Large Glucagon Immunoreactivity in Extracts of Pancreas
The glucagon immunoreactivity present in canine pancreatic extracts can be separated by gel filtration into two fractions; one fraction, comprising over 90% of the immunoreactivity, is similar in molecular size to the glucagon- 131 I marker, while the other appears to be at least twice as large. Inc...
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| Veröffentlicht in: | The Journal of biological chemistry 1970-02, Vol.245 (3), p.496-501 |
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| container_title | The Journal of biological chemistry |
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| creator | Rigopoulou, D Valverde, I Marco, J Faloona, G Unger, R H |
| description | The glucagon immunoreactivity present in canine pancreatic extracts can be separated by gel filtration into two fractions;
one fraction, comprising over 90% of the immunoreactivity, is similar in molecular size to the glucagon- 131 I marker, while the other appears to be at least twice as large. Incubation of this large glucagon immunoreactivity (LGI)
in solutions such as 1 m acetic acid, 8 m urea, 0.1 m mercaptoethanol, or 6 m guanidine hydrochloride, which favor the dissociation of noncovalent protein complexes, fails to change its molecular size
as determined by gel filtration, suggesting that LGI is not glucagon noncovalently bound either to itself or to another protein.
However, tryptic hydrolysis of LGI results in the disappearance of most of the immunoreactivity and in a reduction in the
molecular size of the remaining immunoreactivity to approximately that of glucagon- 131 I. Neither LGI nor its tryptic product, both of which resemble glucagon immunologically, has glycogenolytic activity in the
perfused rat liver. It is possible that LGI includes the immunoreactive sequence of glucagon or of an immunologically similar
peptide. |
| doi_str_mv | 10.1016/S0021-9258(18)63360-5 |
| format | Article |
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one fraction, comprising over 90% of the immunoreactivity, is similar in molecular size to the glucagon- 131 I marker, while the other appears to be at least twice as large. Incubation of this large glucagon immunoreactivity (LGI)
in solutions such as 1 m acetic acid, 8 m urea, 0.1 m mercaptoethanol, or 6 m guanidine hydrochloride, which favor the dissociation of noncovalent protein complexes, fails to change its molecular size
as determined by gel filtration, suggesting that LGI is not glucagon noncovalently bound either to itself or to another protein.
However, tryptic hydrolysis of LGI results in the disappearance of most of the immunoreactivity and in a reduction in the
molecular size of the remaining immunoreactivity to approximately that of glucagon- 131 I. Neither LGI nor its tryptic product, both of which resemble glucagon immunologically, has glycogenolytic activity in the
perfused rat liver. It is possible that LGI includes the immunoreactive sequence of glucagon or of an immunologically similar
peptide.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)63360-5</identifier><identifier>PMID: 5412706</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Acetates ; Animals ; Antigens ; Biological Assay ; Cattle ; Chromatography, Gel ; Dogs ; Ducks ; Electrophoresis, Disc ; Glucagon - analysis ; Glycogen - metabolism ; Guanidines ; Humans ; Immune Sera ; Iodine Isotopes ; Liver - metabolism ; Macromolecular Substances ; Mercaptoethanol ; Pancreas - immunology ; Peptides ; Perfusion ; Radioimmunoassay ; Rats ; Species Specificity ; Swine ; Trypsin ; Urea</subject><ispartof>The Journal of biological chemistry, 1970-02, Vol.245 (3), p.496-501</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c377t-ca679060a6ac3b726ef9c0db728334499c90829bcf24f9af5445339ff2d3a5533</citedby><cites>FETCH-LOGICAL-c377t-ca679060a6ac3b726ef9c0db728334499c90829bcf24f9af5445339ff2d3a5533</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5412706$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rigopoulou, D</creatorcontrib><creatorcontrib>Valverde, I</creatorcontrib><creatorcontrib>Marco, J</creatorcontrib><creatorcontrib>Faloona, G</creatorcontrib><creatorcontrib>Unger, R H</creatorcontrib><title>Large Glucagon Immunoreactivity in Extracts of Pancreas</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The glucagon immunoreactivity present in canine pancreatic extracts can be separated by gel filtration into two fractions;
one fraction, comprising over 90% of the immunoreactivity, is similar in molecular size to the glucagon- 131 I marker, while the other appears to be at least twice as large. Incubation of this large glucagon immunoreactivity (LGI)
in solutions such as 1 m acetic acid, 8 m urea, 0.1 m mercaptoethanol, or 6 m guanidine hydrochloride, which favor the dissociation of noncovalent protein complexes, fails to change its molecular size
as determined by gel filtration, suggesting that LGI is not glucagon noncovalently bound either to itself or to another protein.
However, tryptic hydrolysis of LGI results in the disappearance of most of the immunoreactivity and in a reduction in the
molecular size of the remaining immunoreactivity to approximately that of glucagon- 131 I. Neither LGI nor its tryptic product, both of which resemble glucagon immunologically, has glycogenolytic activity in the
perfused rat liver. It is possible that LGI includes the immunoreactive sequence of glucagon or of an immunologically similar
peptide.</description><subject>Acetates</subject><subject>Animals</subject><subject>Antigens</subject><subject>Biological Assay</subject><subject>Cattle</subject><subject>Chromatography, Gel</subject><subject>Dogs</subject><subject>Ducks</subject><subject>Electrophoresis, Disc</subject><subject>Glucagon - analysis</subject><subject>Glycogen - metabolism</subject><subject>Guanidines</subject><subject>Humans</subject><subject>Immune Sera</subject><subject>Iodine Isotopes</subject><subject>Liver - metabolism</subject><subject>Macromolecular Substances</subject><subject>Mercaptoethanol</subject><subject>Pancreas - immunology</subject><subject>Peptides</subject><subject>Perfusion</subject><subject>Radioimmunoassay</subject><subject>Rats</subject><subject>Species Specificity</subject><subject>Swine</subject><subject>Trypsin</subject><subject>Urea</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1970</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kFtLAzEQhYMotVZ_QmF9EX1YzT2bRym1FgoKKvgWsmnSRrq7NdlV--9NL3ReZoZzzgx8AAwRvEcQ8Yc3CDHKJWbFLSruOCEc5uwE9BEsSE4Y-jwF_aPlHFzE-AVTUYl6oMcowgLyPhAzHRY2m6w6oxdNnU2rqqubYLVp_Y9vN5mvs_FfG9Ies8Zlr7o2SY2X4MzpVbRXhz4AH0_j99FzPnuZTEePs9wQIdrcaC4k5FBzbUgpMLdOGjhPU0EIpVIaCQssS-MwdVI7RikjRDqH50SzNA7Azf7uOjTfnY2tqnw0drXStW26qApKBSVMJCPbG01oYgzWqXXwlQ4bhaDaAlM7YGpLQ6FC7YAplnLDw4OurOz8mDoQSvr1Xl_6xfLXB6tK35ilrRSmTBFFJSf_6opwaQ</recordid><startdate>19700210</startdate><enddate>19700210</enddate><creator>Rigopoulou, D</creator><creator>Valverde, I</creator><creator>Marco, J</creator><creator>Faloona, G</creator><creator>Unger, R H</creator><general>American Society for Biochemistry and Molecular Biology</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>7X8</scope></search><sort><creationdate>19700210</creationdate><title>Large Glucagon Immunoreactivity in Extracts of Pancreas</title><author>Rigopoulou, D ; Valverde, I ; Marco, J ; Faloona, G ; Unger, R H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c377t-ca679060a6ac3b726ef9c0db728334499c90829bcf24f9af5445339ff2d3a5533</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1970</creationdate><topic>Acetates</topic><topic>Animals</topic><topic>Antigens</topic><topic>Biological Assay</topic><topic>Cattle</topic><topic>Chromatography, Gel</topic><topic>Dogs</topic><topic>Ducks</topic><topic>Electrophoresis, Disc</topic><topic>Glucagon - analysis</topic><topic>Glycogen - metabolism</topic><topic>Guanidines</topic><topic>Humans</topic><topic>Immune Sera</topic><topic>Iodine Isotopes</topic><topic>Liver - metabolism</topic><topic>Macromolecular Substances</topic><topic>Mercaptoethanol</topic><topic>Pancreas - immunology</topic><topic>Peptides</topic><topic>Perfusion</topic><topic>Radioimmunoassay</topic><topic>Rats</topic><topic>Species Specificity</topic><topic>Swine</topic><topic>Trypsin</topic><topic>Urea</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rigopoulou, D</creatorcontrib><creatorcontrib>Valverde, I</creatorcontrib><creatorcontrib>Marco, J</creatorcontrib><creatorcontrib>Faloona, G</creatorcontrib><creatorcontrib>Unger, R H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rigopoulou, D</au><au>Valverde, I</au><au>Marco, J</au><au>Faloona, G</au><au>Unger, R H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Large Glucagon Immunoreactivity in Extracts of Pancreas</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1970-02-10</date><risdate>1970</risdate><volume>245</volume><issue>3</issue><spage>496</spage><epage>501</epage><pages>496-501</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The glucagon immunoreactivity present in canine pancreatic extracts can be separated by gel filtration into two fractions;
one fraction, comprising over 90% of the immunoreactivity, is similar in molecular size to the glucagon- 131 I marker, while the other appears to be at least twice as large. Incubation of this large glucagon immunoreactivity (LGI)
in solutions such as 1 m acetic acid, 8 m urea, 0.1 m mercaptoethanol, or 6 m guanidine hydrochloride, which favor the dissociation of noncovalent protein complexes, fails to change its molecular size
as determined by gel filtration, suggesting that LGI is not glucagon noncovalently bound either to itself or to another protein.
However, tryptic hydrolysis of LGI results in the disappearance of most of the immunoreactivity and in a reduction in the
molecular size of the remaining immunoreactivity to approximately that of glucagon- 131 I. Neither LGI nor its tryptic product, both of which resemble glucagon immunologically, has glycogenolytic activity in the
perfused rat liver. It is possible that LGI includes the immunoreactive sequence of glucagon or of an immunologically similar
peptide.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>5412706</pmid><doi>10.1016/S0021-9258(18)63360-5</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1970-02, Vol.245 (3), p.496-501 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Acetates Animals Antigens Biological Assay Cattle Chromatography, Gel Dogs Ducks Electrophoresis, Disc Glucagon - analysis Glycogen - metabolism Guanidines Humans Immune Sera Iodine Isotopes Liver - metabolism Macromolecular Substances Mercaptoethanol Pancreas - immunology Peptides Perfusion Radioimmunoassay Rats Species Specificity Swine Trypsin Urea |
| title | Large Glucagon Immunoreactivity in Extracts of Pancreas |
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