Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/61872
Type: Artigo de periódico
Title: DIMER TETRAMER TRANSITION IN HEMOGLOBIN FROM LIOPHIS-MILIARIS .3. THE PHENOMENON IN SNAKE SPECIES OF DIFFERENT EVOLUTIONARY LEVELS
Author: FOCESI, A
BONILLA, GO
NAGATOMO, CL
MATSUURA, MSA
Abstract: 1. The primitive snake Boa constrictor presents in the stripped hemolysate one component which from O2 equilibrium curves produced the following values: log P50 +/- -0.1 and Hill coefficient n(H) = 1.1, independent of pH. 2. Bothrops alternatus, an evolved snake, presents two components in the hemolysate with functional parameters: log P50 = 0.4 and n(H) = 1.7 at pH 7.5, decreasing to log P50 = -0.1 and n(H) +/- 1.4 at pH 8.2. 3. In the presence of ATP, an increase to log P50 +/- 0.9 and n(H) +/- 2 is found in both snake hemolysates, up to pH 7.8. 4. Molecular weight determinations by gel filtration at pH 8 show only the dimeric form (mol. wt 32,000) in B. constrictor hemolysate, and dimers and tetramers (mol. wt 64,500) in that of B. alternatus. 5. The Hill plots as a function of O2 tension show for B. alternatus hemolysate a shift from deoxytetramer n(H) = 2.02 to oxydimer with n(H) = 0.88 as occurs in L. miliaris. For B. constrictor hemoglobin the n(H) remains 1.0 independent of the O2 tension.
Country: Inglaterra
Editor: Pergamon-elsevier Science Ltd
Rights: fechado
Identifier DOI: 10.1016/0305-0491(92)90227-I
Date Issue: 1992
Appears in Collections:Unicamp - Artigos e Outros Documentos

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