Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/12868
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dc.contributor.authorDrummer, Olaf Hen
dc.contributor.authorKourtis, Sen
dc.contributor.authorJohnson, Hen
dc.date.accessioned2015-05-16T02:37:02Z
dc.date.available2015-05-16T02:37:02Z
dc.date.issued1988-11-15en
dc.identifier.citationBiochemical Pharmacology; 37(22): 4327-33en
dc.identifier.govdoc2848526en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/12868en
dc.description.abstractThe formation of AII from a metabolite of AI, des-leu10-angiotensin I [A(1-9)] has been studied in centrifugal fractions of rat lung and kidney using gradient elution HPLC to monitor the formation of peptide products. AII-forming activity was present in kidney S2 (22.3 nmol/mg protein/min) but not in kidney P2 centrifugal fractions. Lung S2 fractions showed relatively weak AII-forming activity (0.34 nmole/mg protein/min) whilst no activity was observed in lung P2. Carboxypeptidase N-like activity measured using both Hipp-Arg and Hipp-Lys as synthetic substrates did not parallel AII-forming activity, since this activity was highest in the P2 fractions of both lung and kidney, as were ACE and aminopeptidase activities. Whilst the major peptide produced in kidney S2 was AII (71%) significant amounts of both AIII (23%) and A(2-9) (6%) were also observed. In lung the amounts of these peptides produced as a percentage of the A(1-9) degrading activity were 2.9%, 2.4% and 21% respectively. The AII-forming activity in kidney S2 was not inhibited by enalaprilat, bestatin, amastatin, phosphoramidon or Pro-Phe but was inhibited (31%) by 1 mM cobalt (II). 1,10-Phenanthroline, iodoacetic acid, EDTA and puromycin significantly enhanced the formation of AII and increased the rate of degradation of the substrate, A(1-9). These results support the concept of a sequential carboxypeptidase pathway operating, particularly in kidney, to produce AII from AI. These results provide further evidence of an alternative metabolic pathway for the formation of AII not involving angiotensin converting enzyme.en
dc.language.isoenen
dc.subject.otherAminopeptidases.metabolismen
dc.subject.otherAngiotensin I.analogs & derivatives.metabolismen
dc.subject.otherAngiotensin II.metabolismen
dc.subject.otherAnimalsen
dc.subject.otherChromatography, High Pressure Liquiden
dc.subject.otherKidney.metabolismen
dc.subject.otherLung.metabolismen
dc.subject.otherLysine Carboxypeptidase.metabolismen
dc.subject.otherPeptidyl-Dipeptidase A.metabolismen
dc.subject.otherProtease Inhibitors.pharmacologyen
dc.subject.otherRatsen
dc.subject.otherRats, Inbred Strainsen
dc.titleFormation of angiotensin II and other angiotensin peptides from des-leu 10-angiotensin I in rat lung and kidney.en
dc.typeJournal Articleen
dc.identifier.journaltitleBiochemical pharmacologyen
dc.identifier.affiliationUniversity of Melbourne, Austin Hospital, Heidelberg, Victoria, Australiaen
dc.description.pages4327-33en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/2848526en
dc.type.austinJournal Articleen
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairetypeJournal Article-
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