New analogues of secretin
For the evaluation of structure/activity relationships, some porcine secretin analogues, modified in the N-terminus, have been synthesized by segment condensation in solution. The secretin activity of the analogues was defined as the volume of pancreatic juice secreted in rats and dogs. The exchange...
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| Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 1986, Vol.7, p.61-67 |
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| container_title | Peptides (New York, N.Y. : 1980) |
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| creator | König, Wolfgang Bickel, Martin Wissmann, Hans Sandow, Jürgen |
| description | For the evaluation of structure/activity relationships, some porcine secretin analogues, modified in the N-terminus, have been synthesized by segment condensation in solution. The secretin activity of the analogues was defined as the volume of pancreatic juice secreted in rats and dogs. The exchange of the N-terminal pentapeptide for the N-terminal pentapeptide of human somatotropin releasing factor (h-SRF) resulted in a peptide ([1-Tyr,2,4-Di-Ala,5-Ile]secretin) with practically no SRF-activity (less than 1% SRF-activity up to 100 μg/kg in the rat), but surprisingly high secretin activity (almost 100% in the rat, but only 1150 CU/mg (27%) in the dog). [3-L-Cysteic acid]secretin showed 1750 CU/mg (39%) in the dog, but a less activity (23%) in the rat. [6-D-Phe]secretin and [5-D-allo-Thr]secretin are again strongly species specific. They exhibited an activity of less than 1% in the dog, but about 10–15% in the rat. The smallest secretin activity was observed with [1-Cys,6-Cys]secretin in the oxidized form. The activity in the rat with this analogue was only about 0.2%. |
| doi_str_mv | 10.1016/0196-9781(86)90165-8 |
| format | Article |
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The secretin activity of the analogues was defined as the volume of pancreatic juice secreted in rats and dogs. The exchange of the N-terminal pentapeptide for the N-terminal pentapeptide of human somatotropin releasing factor (h-SRF) resulted in a peptide ([1-Tyr,2,4-Di-Ala,5-Ile]secretin) with practically no SRF-activity (less than 1% SRF-activity up to 100 μg/kg in the rat), but surprisingly high secretin activity (almost 100% in the rat, but only 1150 CU/mg (27%) in the dog). [3-L-Cysteic acid]secretin showed 1750 CU/mg (39%) in the dog, but a less activity (23%) in the rat. [6-D-Phe]secretin and [5-D-allo-Thr]secretin are again strongly species specific. They exhibited an activity of less than 1% in the dog, but about 10–15% in the rat. The smallest secretin activity was observed with [1-Cys,6-Cys]secretin in the oxidized form. The activity in the rat with this analogue was only about 0.2%.</description><identifier>ISSN: 0196-9781</identifier><identifier>EISSN: 1873-5169</identifier><identifier>DOI: 10.1016/0196-9781(86)90165-8</identifier><identifier>PMID: 3092198</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Dogs ; Growth Hormone - metabolism ; Growth Hormone-Releasing Hormone - analogs & derivatives ; Male ; Pancreatic Juice - drug effects ; Pancreatic Juice - metabolism ; Rats ; Secretin ; Secretin - analogs & derivatives ; Secretin - chemical synthesis ; Secretin - pharmacology ; Secretin analogues ; Somatotropin releasing factor analogues ; Species Specificity ; Structure-Activity Relationship</subject><ispartof>Peptides (New York, N.Y. : 1980), 1986, Vol.7, p.61-67</ispartof><rights>1986</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-6d77d6da55165d28e7dfcd14f2c8e84c8afc4f9c5637999a94df82d72f59acf63</citedby><cites>FETCH-LOGICAL-c357t-6d77d6da55165d28e7dfcd14f2c8e84c8afc4f9c5637999a94df82d72f59acf63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0196978186901658$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,4009,27902,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3092198$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>König, Wolfgang</creatorcontrib><creatorcontrib>Bickel, Martin</creatorcontrib><creatorcontrib>Wissmann, Hans</creatorcontrib><creatorcontrib>Sandow, Jürgen</creatorcontrib><title>New analogues of secretin</title><title>Peptides (New York, N.Y. : 1980)</title><addtitle>Peptides</addtitle><description>For the evaluation of structure/activity relationships, some porcine secretin analogues, modified in the N-terminus, have been synthesized by segment condensation in solution. The secretin activity of the analogues was defined as the volume of pancreatic juice secreted in rats and dogs. The exchange of the N-terminal pentapeptide for the N-terminal pentapeptide of human somatotropin releasing factor (h-SRF) resulted in a peptide ([1-Tyr,2,4-Di-Ala,5-Ile]secretin) with practically no SRF-activity (less than 1% SRF-activity up to 100 μg/kg in the rat), but surprisingly high secretin activity (almost 100% in the rat, but only 1150 CU/mg (27%) in the dog). [3-L-Cysteic acid]secretin showed 1750 CU/mg (39%) in the dog, but a less activity (23%) in the rat. [6-D-Phe]secretin and [5-D-allo-Thr]secretin are again strongly species specific. They exhibited an activity of less than 1% in the dog, but about 10–15% in the rat. The smallest secretin activity was observed with [1-Cys,6-Cys]secretin in the oxidized form. The activity in the rat with this analogue was only about 0.2%.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Dogs</subject><subject>Growth Hormone - metabolism</subject><subject>Growth Hormone-Releasing Hormone - analogs & derivatives</subject><subject>Male</subject><subject>Pancreatic Juice - drug effects</subject><subject>Pancreatic Juice - metabolism</subject><subject>Rats</subject><subject>Secretin</subject><subject>Secretin - analogs & derivatives</subject><subject>Secretin - chemical synthesis</subject><subject>Secretin - pharmacology</subject><subject>Secretin analogues</subject><subject>Somatotropin releasing factor analogues</subject><subject>Species Specificity</subject><subject>Structure-Activity Relationship</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>eNp9UE1LAzEUDKLUWv0BgkJPoofVJJvPS0GKX1D0oucQkxeJbHdrslX892Zp6dHTwHsz894MQmcEXxNMxA0mWlRaKnKpxJUuE16pPTQmStYVJ0Lvo_GOcoiOcv7EGDOm1QiNaqwp0WqMTp_hZ2pb23Qfa8jTLkwzuAR9bI_RQbBNhpMtTtDb_d3r_LFavDw8zW8Xlau57CvhpfTCW15Ock8VSB-cJyxQp0Axp2xwLGjHRS211lYzHxT1kgaurQuinqCLje8qdV_lh94sY3bQNLaFbp2NlJhwSutCZBuiS13OCYJZpbi06dcQbIZGzBDXDHGNKjg0YlSRnW_91-9L8DvRtoKyn232UEJ-R0gmuwitAx8TuN74Lv5_4A_SFW50</recordid><startdate>1986</startdate><enddate>1986</enddate><creator>König, Wolfgang</creator><creator>Bickel, Martin</creator><creator>Wissmann, Hans</creator><creator>Sandow, Jürgen</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>7X8</scope></search><sort><creationdate>1986</creationdate><title>New analogues of secretin</title><author>König, Wolfgang ; Bickel, Martin ; Wissmann, Hans ; Sandow, Jürgen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-6d77d6da55165d28e7dfcd14f2c8e84c8afc4f9c5637999a94df82d72f59acf63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Dogs</topic><topic>Growth Hormone - metabolism</topic><topic>Growth Hormone-Releasing Hormone - analogs & derivatives</topic><topic>Male</topic><topic>Pancreatic Juice - drug effects</topic><topic>Pancreatic Juice - metabolism</topic><topic>Rats</topic><topic>Secretin</topic><topic>Secretin - analogs & derivatives</topic><topic>Secretin - chemical synthesis</topic><topic>Secretin - pharmacology</topic><topic>Secretin analogues</topic><topic>Somatotropin releasing factor analogues</topic><topic>Species Specificity</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>König, Wolfgang</creatorcontrib><creatorcontrib>Bickel, Martin</creatorcontrib><creatorcontrib>Wissmann, Hans</creatorcontrib><creatorcontrib>Sandow, Jürgen</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>Peptides (New York, N.Y. : 1980)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>König, Wolfgang</au><au>Bickel, Martin</au><au>Wissmann, Hans</au><au>Sandow, Jürgen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>New analogues of secretin</atitle><jtitle>Peptides (New York, N.Y. : 1980)</jtitle><addtitle>Peptides</addtitle><date>1986</date><risdate>1986</risdate><volume>7</volume><spage>61</spage><epage>67</epage><pages>61-67</pages><issn>0196-9781</issn><eissn>1873-5169</eissn><abstract>For the evaluation of structure/activity relationships, some porcine secretin analogues, modified in the N-terminus, have been synthesized by segment condensation in solution. The secretin activity of the analogues was defined as the volume of pancreatic juice secreted in rats and dogs. The exchange of the N-terminal pentapeptide for the N-terminal pentapeptide of human somatotropin releasing factor (h-SRF) resulted in a peptide ([1-Tyr,2,4-Di-Ala,5-Ile]secretin) with practically no SRF-activity (less than 1% SRF-activity up to 100 μg/kg in the rat), but surprisingly high secretin activity (almost 100% in the rat, but only 1150 CU/mg (27%) in the dog). [3-L-Cysteic acid]secretin showed 1750 CU/mg (39%) in the dog, but a less activity (23%) in the rat. [6-D-Phe]secretin and [5-D-allo-Thr]secretin are again strongly species specific. They exhibited an activity of less than 1% in the dog, but about 10–15% in the rat. The smallest secretin activity was observed with [1-Cys,6-Cys]secretin in the oxidized form. The activity in the rat with this analogue was only about 0.2%.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>3092198</pmid><doi>10.1016/0196-9781(86)90165-8</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0196-9781 |
| ispartof | Peptides (New York, N.Y. : 1980), 1986, Vol.7, p.61-67 |
| issn | 0196-9781 1873-5169 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77015223 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Animals Dogs Growth Hormone - metabolism Growth Hormone-Releasing Hormone - analogs & derivatives Male Pancreatic Juice - drug effects Pancreatic Juice - metabolism Rats Secretin Secretin - analogs & derivatives Secretin - chemical synthesis Secretin - pharmacology Secretin analogues Somatotropin releasing factor analogues Species Specificity Structure-Activity Relationship |
| title | New analogues of secretin |
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