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Article: Structure-function relationships in glucagon: Properties of highly purified des-His1-, monoiodo-, and [des-Asn 28,Thr 29](homoserine lactone 27)-glucagon

TitleStructure-function relationships in glucagon: Properties of highly purified des-His1-, monoiodo-, and [des-Asn 28,Thr 29](homoserine lactone 27)-glucagon
Authors
Issue Date1975
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistry
Citation
Biochemistry, 1975, v. 14 n. 8, p. 1559-1563 How to Cite?
AbstractWe have compared the ability of glucagon and three highly purified derivatives of the hormone to activate hepatic adenylate cyclase (an expression of biological activity of the hormone) and to compete with [ 125] glucagon for binding to sites specific for glucagon in hepatic plasma membranes. Relative to that of glucagon, biological activity and affinity of [des-Asn 28,Thr 29](homoserine lactone 27)-glucagon, prepared by CNBr treatment of glucagon, were reduced equally by 40- to 50-fold. By contrast, des-His 1-glucagon, prepared by an insoluble Edman reagent and highly purified (less than 0.5% contamination with native glucagon), displayed a 15-fold decrease in affinity but a 50-fold decrease in biological activity relative to that of the native hormone. At maximal stimulating concentrations, des-His 1-glucagon yielded 70% of the activity given by saturating concentrations of glucagon. Thus, des-His 1-glucagon can be classified as a partial, weak agonist. Highly purified monoiodoglucagon and native glucagon displayed identical biological activity and affinity for the binding sites. Our findings suggest that the hydrophilic residues at the terminus of the carboxy region of glucagon are involved in the process of recognition at the glucagon receptor but do not participate in the sequence of events leading to activation of adenylate cyclase. The amino-terminal histidyl residue in glucagon plays an important but not obligatory role in the expression of hormone action and contributes to a significant extent in the recognition process.
Persistent Identifierhttp://hdl.handle.net/10722/167433
ISSN
2015 Impact Factor: 2.876
2015 SCImago Journal Rankings: 1.769
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLin, MCen_US
dc.contributor.authorWright, DEen_US
dc.contributor.authorHruby, VJen_US
dc.contributor.authorRodbell, Men_US
dc.date.accessioned2012-10-08T03:06:55Z-
dc.date.available2012-10-08T03:06:55Z-
dc.date.issued1975en_US
dc.identifier.citationBiochemistry, 1975, v. 14 n. 8, p. 1559-1563en_US
dc.identifier.issn0006-2960en_US
dc.identifier.urihttp://hdl.handle.net/10722/167433-
dc.description.abstractWe have compared the ability of glucagon and three highly purified derivatives of the hormone to activate hepatic adenylate cyclase (an expression of biological activity of the hormone) and to compete with [ 125] glucagon for binding to sites specific for glucagon in hepatic plasma membranes. Relative to that of glucagon, biological activity and affinity of [des-Asn 28,Thr 29](homoserine lactone 27)-glucagon, prepared by CNBr treatment of glucagon, were reduced equally by 40- to 50-fold. By contrast, des-His 1-glucagon, prepared by an insoluble Edman reagent and highly purified (less than 0.5% contamination with native glucagon), displayed a 15-fold decrease in affinity but a 50-fold decrease in biological activity relative to that of the native hormone. At maximal stimulating concentrations, des-His 1-glucagon yielded 70% of the activity given by saturating concentrations of glucagon. Thus, des-His 1-glucagon can be classified as a partial, weak agonist. Highly purified monoiodoglucagon and native glucagon displayed identical biological activity and affinity for the binding sites. Our findings suggest that the hydrophilic residues at the terminus of the carboxy region of glucagon are involved in the process of recognition at the glucagon receptor but do not participate in the sequence of events leading to activation of adenylate cyclase. The amino-terminal histidyl residue in glucagon plays an important but not obligatory role in the expression of hormone action and contributes to a significant extent in the recognition process.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistryen_US
dc.relation.ispartofBiochemistryen_US
dc.titleStructure-function relationships in glucagon: Properties of highly purified des-His1-, monoiodo-, and [des-Asn 28,Thr 29](homoserine lactone 27)-glucagonen_US
dc.typeArticleen_US
dc.identifier.emailLin, MC:mcllin@hkucc.hku.hken_US
dc.identifier.authorityLin, MC=rp00746en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/bi00679a002-
dc.identifier.pmid164891-
dc.identifier.scopuseid_2-s2.0-0016681633en_US
dc.identifier.volume14en_US
dc.identifier.issue8en_US
dc.identifier.spage1559en_US
dc.identifier.epage1563en_US
dc.identifier.isiWOS:A1975W280600002-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLin, MC=7404816359en_US
dc.identifier.scopusauthoridWright, DE=7404381610en_US
dc.identifier.scopusauthoridHruby, VJ=36077273000en_US
dc.identifier.scopusauthoridRodbell, M=7006658086en_US

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