dc.creator | Cardillo, F | |
dc.creator | de Paula, E | |
dc.creator | Oliveira, G R | |
dc.creator | Marangoni, S | |
dc.creator | Oliveira, B | |
dc.creator | Meirelles, N C | |
dc.date | 1997-Mar | |
dc.date | 2015-11-27T12:18:55Z | |
dc.date | 2015-11-27T12:18:55Z | |
dc.date.accessioned | 2018-03-29T00:52:09Z | |
dc.date.available | 2018-03-29T00:52:09Z | |
dc.identifier | Biochemistry And Molecular Biology International. v. 41, n. 3, p. 497-509, 1997-Mar. | |
dc.identifier | 1039-9712 | |
dc.identifier | | |
dc.identifier | http://www.ncbi.nlm.nih.gov/pubmed/9090457 | |
dc.identifier | http://repositorio.unicamp.br/jspui/handle/REPOSIP/194013 | |
dc.identifier | 9090457 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1294246 | |
dc.description | 1) 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.description | 41 | |
dc.description | 497-509 | |
dc.language | eng | |
dc.relation | Biochemistry And Molecular Biology International | |
dc.relation | Biochem. Mol. Biol. Int. | |
dc.rights | fechado | |
dc.rights | | |
dc.source | PubMed | |
dc.subject | Animals | |
dc.subject | Antibodies | |
dc.subject | Chromatography, Deae-cellulose | |
dc.subject | Hemoglobins | |
dc.subject | Humans | |
dc.subject | Immunoelectrophoresis | |
dc.subject | Immunoglobulin Fab Fragments | |
dc.subject | Immunoglobulin G | |
dc.subject | Oligochaeta | |
dc.subject | Oxygen | |
dc.subject | Protein Conformation | |
dc.subject | Rabbits | |
dc.subject | Serum Albumin | |
dc.title | Erythrocruorin Of Glossoscolex Paulistus (oligochaeta, Glossoscolecidae): Modulation Of Oxygen Affinity By Specific Antibodies. | |
dc.type | Artículos de revistas | |