Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/11262
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dc.contributor.authorWaugh, R.-
dc.contributor.authorSteinborner, S.-
dc.contributor.authorBowie, J.-
dc.contributor.authorWallace, J.-
dc.contributor.authorTyler, M.-
dc.contributor.authorHu, P.-
dc.contributor.authorGross, M.-
dc.date.issued1995-
dc.identifier.citationAustralian Journal of Chemistry: an international journal for chemical science, 1995; 48(12):1981-1987-
dc.identifier.issn0004-9425-
dc.identifier.issn1445-0038-
dc.identifier.urihttp://hdl.handle.net/2440/11262-
dc.description.abstract<jats:p>Three related peptides, caeridins 1.1-1.3, have been isolated from the green tree frog Litoria gilleni. Caeridins 1.1 and 1.2 are dodecapeptides differing only in having α and β Asp at residue 4 [viz. Gly Leu Leu Asp Gly Leu Leu Gly Thr Leu Gly Leu (NH2)]. Caeridin 1.3 is the corresponding cyclic amino succinyl derivative derived formally by cyclization of Asp(4) and Gly (5). Hydrolysis of caeridin 1.3 yields caeridin 1.1 and 1.2 in the ratio 3:1. This constitutes a rare case of the isolation of three such related peptides from a natural system. </jats:p>-
dc.description.urihttp://www.publish.csiro.au/nid/51/paper/CH9951981.htm-
dc.language.isoen-
dc.publisherCSIRO-
dc.source.urihttp://dx.doi.org/10.1071/ch9951981-
dc.titleTwo isomeric a and b aspartyl dodecapeptides and their cyclic amino succinyl analogues from the Australian Green Tree Frog Litoria gilleni-
dc.typeJournal article-
dc.identifier.doi10.1071/CH9951981-
pubs.publication-statusPublished-
Appears in Collections:Aurora harvest 2
Biochemistry publications

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