Literature DB >> 7213659

Root effect of Panulirus interruptus hemocyanin.

H A Kuiper, M Coletta, L Zolla, E Chiancone, M Brunori.   

Abstract

Panulirus interruptus hemocyanin exhibits a progressive decrease in oxygen affinity and a parallel loss of cooperativity with decrease in pH, resulting in an apparent loss of the oxygen-binding capacity of the protein. For a characterization of this system, oxygen-binding curves have been determined over the complete range of oxygen saturation, applying a special technique which involves high-pressure spectrophotometry. Although the oxygen-binding behavior as a function of pH is complex and cannot be described within the frame of a simple two-state Monod-Wyman-Changeux model, the observed Root effect is clearly related to a progressive stabilization of a low oxygen affinity state of the protein and functional heterogeneity is not apparent.

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Year:  1980        PMID: 7213659     DOI: 10.1016/0005-2795(80)90136-1

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  An investigation of the nature of Bohr, Root, and Haldane effects in Octopus dofleini hemocyanin.

Authors:  K I Miller; C P Mangum
Journal:  J Comp Physiol B       Date:  1988       Impact factor: 2.200

2.  Molecular basis of the Bohr effect in arthropod hemocyanin.

Authors:  Shun Hirota; Takumi Kawahara; Mariano Beltramini; Paolo Di Muro; Richard S Magliozzo; Jack Peisach; Linda S Powers; Naoki Tanaka; Satoshi Nagao; Luigi Bubacco
Journal:  J Biol Chem       Date:  2008-08-25       Impact factor: 5.157

  2 in total

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