Relative bioactivities of cholecystokinins-8 and -33 on rat pancreatic acini
The relative potencies of cholecystokinin (CCK-33) and its carboxyl terminal octapeptide (CCK-8) for stimulation of amylase release from rat pancreatic acini was measured. Porcine CCK-33 and synthetic CCK-8 were initially subjected to high pressure liquid chromatography to assess purity. Concentrati...
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| Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 1986-09, Vol.7 (5), p.723-727 |
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| container_title | Peptides (New York, N.Y. : 1980) |
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| creator | Liddle, Rodger A. Elashoff, Janet Reeve, Joseph R. |
| description | The relative potencies of cholecystokinin (CCK-33) and its carboxyl terminal octapeptide (CCK-8) for stimulation of amylase release from rat pancreatic acini was measured. Porcine CCK-33 and synthetic CCK-8 were initially subjected to high pressure liquid chromatography to assess purity. Concentrations of each peptide were determined by amino acid analysis. The relative immunoreactivities of CCK-33 and CCK-8 were compared using an antibody that recognizes the common carboxyl terminus of these forms. This antibody bound CCK-8 and CCK-33 with nearly equal affinity. The relative potencies of CCK-33 and CCK-8 were then measured by comparing their abilities to stimulate amylase release from isolated rat pancreatic acini. Statistical analysis of the relative potencies of the two hormones indicated that CCK-8 was 36% more potent than CCK-33 in this assay system. These data suggest that differences in biological activities between large and small forms of CCK are not as great as previously reported. |
| doi_str_mv | 10.1016/0196-9781(86)90085-9 |
| format | Article |
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Porcine CCK-33 and synthetic CCK-8 were initially subjected to high pressure liquid chromatography to assess purity. Concentrations of each peptide were determined by amino acid analysis. The relative immunoreactivities of CCK-33 and CCK-8 were compared using an antibody that recognizes the common carboxyl terminus of these forms. This antibody bound CCK-8 and CCK-33 with nearly equal affinity. The relative potencies of CCK-33 and CCK-8 were then measured by comparing their abilities to stimulate amylase release from isolated rat pancreatic acini. Statistical analysis of the relative potencies of the two hormones indicated that CCK-8 was 36% more potent than CCK-33 in this assay system. These data suggest that differences in biological activities between large and small forms of CCK are not as great as previously reported.</description><identifier>ISSN: 0196-9781</identifier><identifier>EISSN: 1873-5169</identifier><identifier>DOI: 10.1016/0196-9781(86)90085-9</identifier><identifier>PMID: 2432584</identifier><identifier>CODEN: PPTDD5</identifier><language>eng</language><publisher>New York, NY: Elsevier Inc</publisher><subject>Amino acid analysis ; Amino Acids - analysis ; Amylases - metabolism ; Animals ; Bioactivity ; Biological and medical sciences ; Cholecystokinin ; Cholecystokinin - pharmacology ; Exocrine pancreas ; Fundamental and applied biological sciences. Psychology ; HPLC ; Molecular forms ; Pancreas ; Pancreas - enzymology ; Pancreatic Juice - drug effects ; Pancreatic Juice - metabolism ; Radioimmunoassay ; Rats ; Sincalide - pharmacology ; Vertebrates: digestive system</subject><ispartof>Peptides (New York, N.Y. : 1980), 1986-09, Vol.7 (5), p.723-727</ispartof><rights>1986</rights><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c332t-aa95c940cebc231b0bbf25e332ad67f243dccaabe952c26694400db51d46f9313</citedby><cites>FETCH-LOGICAL-c332t-aa95c940cebc231b0bbf25e332ad67f243dccaabe952c26694400db51d46f9313</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0196978186900859$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8266062$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2432584$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liddle, Rodger A.</creatorcontrib><creatorcontrib>Elashoff, Janet</creatorcontrib><creatorcontrib>Reeve, Joseph R.</creatorcontrib><title>Relative bioactivities of cholecystokinins-8 and -33 on rat pancreatic acini</title><title>Peptides (New York, N.Y. : 1980)</title><addtitle>Peptides</addtitle><description>The relative potencies of cholecystokinin (CCK-33) and its carboxyl terminal octapeptide (CCK-8) for stimulation of amylase release from rat pancreatic acini was measured. Porcine CCK-33 and synthetic CCK-8 were initially subjected to high pressure liquid chromatography to assess purity. Concentrations of each peptide were determined by amino acid analysis. The relative immunoreactivities of CCK-33 and CCK-8 were compared using an antibody that recognizes the common carboxyl terminus of these forms. This antibody bound CCK-8 and CCK-33 with nearly equal affinity. The relative potencies of CCK-33 and CCK-8 were then measured by comparing their abilities to stimulate amylase release from isolated rat pancreatic acini. Statistical analysis of the relative potencies of the two hormones indicated that CCK-8 was 36% more potent than CCK-33 in this assay system. These data suggest that differences in biological activities between large and small forms of CCK are not as great as previously reported.</description><subject>Amino acid analysis</subject><subject>Amino Acids - analysis</subject><subject>Amylases - metabolism</subject><subject>Animals</subject><subject>Bioactivity</subject><subject>Biological and medical sciences</subject><subject>Cholecystokinin</subject><subject>Cholecystokinin - pharmacology</subject><subject>Exocrine pancreas</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HPLC</subject><subject>Molecular forms</subject><subject>Pancreas</subject><subject>Pancreas - enzymology</subject><subject>Pancreatic Juice - drug effects</subject><subject>Pancreatic Juice - metabolism</subject><subject>Radioimmunoassay</subject><subject>Rats</subject><subject>Sincalide - pharmacology</subject><subject>Vertebrates: digestive system</subject><issn>0196-9781</issn><issn>1873-5169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LJDEQhoO46Oj6DxRykEUPvZuvTicXYRE_FgYWRM8hXV2N0Z7OmPQI_nszzDBHPVXgfd6i8hByytlvzrj-w7jVlW0MvzD60jJm6srukRk3jaxqru0-me2QQ3KU8wtjTClrDsiBUFLURs3I_AEHP4V3pG2IHsorTAEzjT2F5zggfOQpvoYxjLky1I8draSkcaTJT3TpR0hY6kA9FOYn-dH7IePJdh6Tp9ubx-v7av7_7t_133kFUoqp8t7WYBUDbEFI3rK27UWNJfOdbvpyWwfgfYu2FiC0tkox1rU175TureTymPza7F2m-LbCPLlFyIDD4EeMq-yaRght-fcgV0UCt3UB1QaEFHNO2LtlCgufPhxnbm3brVW6tUpnylzbdrbUzrb7V-0Cu11pq7fk59vcZ_BDn4qwkHeYKZ9jWhTsaoNhkfYeMLkMAUfALiSEyXUxfH3HJ9FDmoA</recordid><startdate>198609</startdate><enddate>198609</enddate><creator>Liddle, Rodger A.</creator><creator>Elashoff, Janet</creator><creator>Reeve, Joseph R.</creator><general>Elsevier Inc</general><general>Elsevier Science</general><scope>IQODW</scope><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>7TK</scope><scope>7X8</scope></search><sort><creationdate>198609</creationdate><title>Relative bioactivities of cholecystokinins-8 and -33 on rat pancreatic acini</title><author>Liddle, Rodger A. ; Elashoff, Janet ; Reeve, Joseph R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c332t-aa95c940cebc231b0bbf25e332ad67f243dccaabe952c26694400db51d46f9313</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Amino acid analysis</topic><topic>Amino Acids - analysis</topic><topic>Amylases - metabolism</topic><topic>Animals</topic><topic>Bioactivity</topic><topic>Biological and medical sciences</topic><topic>Cholecystokinin</topic><topic>Cholecystokinin - pharmacology</topic><topic>Exocrine pancreas</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>HPLC</topic><topic>Molecular forms</topic><topic>Pancreas</topic><topic>Pancreas - enzymology</topic><topic>Pancreatic Juice - drug effects</topic><topic>Pancreatic Juice - metabolism</topic><topic>Radioimmunoassay</topic><topic>Rats</topic><topic>Sincalide - pharmacology</topic><topic>Vertebrates: digestive system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liddle, Rodger A.</creatorcontrib><creatorcontrib>Elashoff, Janet</creatorcontrib><creatorcontrib>Reeve, Joseph R.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Peptides (New York, N.Y. : 1980)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liddle, Rodger A.</au><au>Elashoff, Janet</au><au>Reeve, Joseph R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Relative bioactivities of cholecystokinins-8 and -33 on rat pancreatic acini</atitle><jtitle>Peptides (New York, N.Y. : 1980)</jtitle><addtitle>Peptides</addtitle><date>1986-09</date><risdate>1986</risdate><volume>7</volume><issue>5</issue><spage>723</spage><epage>727</epage><pages>723-727</pages><issn>0196-9781</issn><eissn>1873-5169</eissn><coden>PPTDD5</coden><abstract>The relative potencies of cholecystokinin (CCK-33) and its carboxyl terminal octapeptide (CCK-8) for stimulation of amylase release from rat pancreatic acini was measured. Porcine CCK-33 and synthetic CCK-8 were initially subjected to high pressure liquid chromatography to assess purity. Concentrations of each peptide were determined by amino acid analysis. The relative immunoreactivities of CCK-33 and CCK-8 were compared using an antibody that recognizes the common carboxyl terminus of these forms. This antibody bound CCK-8 and CCK-33 with nearly equal affinity. The relative potencies of CCK-33 and CCK-8 were then measured by comparing their abilities to stimulate amylase release from isolated rat pancreatic acini. Statistical analysis of the relative potencies of the two hormones indicated that CCK-8 was 36% more potent than CCK-33 in this assay system. These data suggest that differences in biological activities between large and small forms of CCK are not as great as previously reported.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>2432584</pmid><doi>10.1016/0196-9781(86)90085-9</doi><tpages>5</tpages></addata></record> |
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| identifier | ISSN: 0196-9781 |
| ispartof | Peptides (New York, N.Y. : 1980), 1986-09, Vol.7 (5), p.723-727 |
| issn | 0196-9781 1873-5169 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino acid analysis Amino Acids - analysis Amylases - metabolism Animals Bioactivity Biological and medical sciences Cholecystokinin Cholecystokinin - pharmacology Exocrine pancreas Fundamental and applied biological sciences. Psychology HPLC Molecular forms Pancreas Pancreas - enzymology Pancreatic Juice - drug effects Pancreatic Juice - metabolism Radioimmunoassay Rats Sincalide - pharmacology Vertebrates: digestive system |
| title | Relative bioactivities of cholecystokinins-8 and -33 on rat pancreatic acini |
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