dc.creatorCardillo, F
dc.creatorde Paula, E
dc.creatorOliveira, G R
dc.creatorMarangoni, S
dc.creatorOliveira, B
dc.creatorMeirelles, N C
dc.date1997-Mar
dc.date2015-11-27T12:18:55Z
dc.date2015-11-27T12:18:55Z
dc.date.accessioned2018-03-29T00:52:09Z
dc.date.available2018-03-29T00:52:09Z
dc.identifierBiochemistry And Molecular Biology International. v. 41, n. 3, p. 497-509, 1997-Mar.
dc.identifier1039-9712
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/9090457
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194013
dc.identifier9090457
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294246
dc.description1) The Soret region absorption spectrum of erythrocruorin (ERC) obtained from Glossoscolex paulistus, shows that oxy-ERC has a maximum absorption peak at 416 nm while the deoxy-ERC from has a maximum at 427 nm. 2) In the presence of a specific antiserum (anti-ERC) and of anti-ERC immunoglobulin G raised in rabbits, there is a deviation to low wavelengths in the maximum absorption peak of deoxy-ERC while for the oxy form a red-shift is noticed. These shifts accompanied an increased affinity of the hemeprotein for oxygen, possibly because of changes in the overall macromolecular conformation. 3) A decrease in the oxygen affinity of erythrocruorin is observed when large amounts of non-specific serum are used. The same effect is observed in the presence of serum albumin, probably as a result of non-specific binding between the albumin and erythrocruorin. 4) The fluorimetric titration of erythrocruorin with anti-ERC Fab fragments results in a decrease in the intrinsic tryptophan fluorescence of the hemeprotein, a response indicative of a modification in the ERC's quaternary structure.
dc.description41
dc.description497-509
dc.languageeng
dc.relationBiochemistry And Molecular Biology International
dc.relationBiochem. Mol. Biol. Int.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAnimals
dc.subjectAntibodies
dc.subjectChromatography, Deae-cellulose
dc.subjectHemoglobins
dc.subjectHumans
dc.subjectImmunoelectrophoresis
dc.subjectImmunoglobulin Fab Fragments
dc.subjectImmunoglobulin G
dc.subjectOligochaeta
dc.subjectOxygen
dc.subjectProtein Conformation
dc.subjectRabbits
dc.subjectSerum Albumin
dc.titleErythrocruorin Of Glossoscolex Paulistus (oligochaeta, Glossoscolecidae): Modulation Of Oxygen Affinity By Specific Antibodies.
dc.typeArtículos de revistas


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