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Hemocyanin oxygen-binding properties of a deep-sea hydrothermal vent shrimp: Evidence for a novel cofactor

1997; Wiley; Volume: 277; Issue: 5 Linguagem: Inglês

10.1002/(sici)1097-010x(19970401)277

1097-010X

François H. Lallier, J.P. Truchot,

Crustacean biology and ecology

Journal of Experimental ZoologyVolume 277, Issue 5 p. 357-364 Comparative Physiology and Biochemistry Hemocyanin oxygen-binding properties of a deep-sea hydrothermal vent shrimp: Evidence for a novel cofactor F. H. Lallier, Corresponding Author F. H. Lallier Equipe Ecophysiologie, UPMC-CNRS-INSU, Station Biologique, 29682 Roscoff Cedex, FranceStation Biologique, Place Georges Teissier, BP 74, 29682 Roscoff Cedex, France===Search for more papers by this authorJ.-P. Truchot, J.-P. Truchot Laboratoire de Neurobiologie et Physiologie Comparées, CNRS URA 1126, 33120 Arcachon, FranceSearch for more papers by this author F. H. Lallier, Corresponding Author F. H. Lallier Equipe Ecophysiologie, UPMC-CNRS-INSU, Station Biologique, 29682 Roscoff Cedex, FranceStation Biologique, Place Georges Teissier, BP 74, 29682 Roscoff Cedex, France===Search for more papers by this authorJ.-P. Truchot, J.-P. Truchot Laboratoire de Neurobiologie et Physiologie Comparées, CNRS URA 1126, 33120 Arcachon, FranceSearch for more papers by this author First published: 07 December 1998 https://doi.org/10.1002/(SICI)1097-010X(19970401)277:5 3.0.CO;2-OCitations: 18AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract Rimicaris exoculata is a caridean shrimp from the family Alvinocarididae which forms the dominant species around deep-sea hydrothermal vents from the Mid-Atlantic Ridge (MAR). Seeking respiratory adaptations to the hydrothermal environment, we have analysed the oxygen-binding properties of Rimicaris hemocyanin (Hc) in relation with temperature, pH, and lactate variations. Rimicaris native Hc is mostly composed of hexamers. It showed a high oxygen affinity (P50 approximately 3 Torr at pH 7.5, 15°C), a large Bohr effect (ΔlogP50/ΔpH = −1.87 ± 0.25, n = 6), a moderate lactate effect (ΔP50/Δlog[lac] = −0.12) and almost no temperature effect (ΔH = −1.23 kJ.mol−1 15–35°C). Most surprisingly, dialysis of native hemolymph elicited a large increase of HC-O2 affinity, an effect opposite to the usual trend observed for crustacean Hcs. Moreover, this increase in affinity could be reversed by adding an ultrafiltrate of native hemolymph to a dialysed sample, thus unveiling the existence of a dialysable yet unknown cofactor which decreases Hc-oxygen affinity. J. Exp. Zool. 277:357–364, 1997. © 1997 Wiley-Liss, Inc. Citing Literature Volume277, Issue51 April 1997Pages 357-364 RelatedInformation