{"refrec":{"BRefID":67003,"RR":"<b>Zal, F.; Leize, E.; Oros, D.R.; Hourdez, S.; Van Dorsselaer, A.; Childress, J.J.</b> (2000). Haemoglobin structure and biochemical characteristics of the sulphide-binding component from the deep-sea clam <i>Calyptogena magnifica</i>. <i>Cah. Biol. Mar. 41(4)</i>: 413-423","BEntID":63370,"PublicFlag":1,"CheckedFlag":0,"wosflag":1,"vabbflag":null,"RefStringPartII":". <i>Cah. Biol. Mar. 41(4)</i>: 413-423","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Zal, F.; Leize, E.; Oros, D.R.; Hourdez, S.; Van Dorsselaer, A.; Childress, J.J.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Zal, F. <i>et al.</i>","Englishabstract":"<i>Calyptogena magnifica</i> is a large heterodont clam belonging to the family vesicomyidae that lives at a depth of ca. 2600 m, near deep-sea hydrothermal vent areas on the East-Pacific Rise and Galapagos Rift. This species harbors abundant autotrophic sulphide-oxidizing bacteria contained in bacteriocytes and located in the gills. Unlike the tube worm <i>Riftia pachyptila</i>, which possesses extracellular haemoglobins that bind sulphide and oxygen simultaneously and reversibly at two different sites, <i>Calyptogena magnifica</i> possesses in its haemolymph two different types of molecules for these functions: an intracellular circulating haemoglobin (Hb) for oxygen binding and a sulphide-binding component (SBC) dissolved in the serum. To elucidate its quaternary structure, the haemoglobin was purified by gel chromatography (FPLC) and then analysed by electrospray ionization mass spectrometry (ESI-MS). FPLC analysis revealed a molecular mass of approximately 68 kDa. By mass spectrometry, under native condition, we found that this molecule contains two subunits of molecular masses 16134.0 Da (alpha ) and 32513.1 Da (beta gamma). After reduction, the beta gamma ubunit corresponds to a covalent heterodimer consisting of chains beta and gamma with Mr of 16148.0_and 16371.0, respectively. Our data suggest that <i>C. magnifica</i> intracellular Hb is a tetrameric molecule with three possible associations: (beta gamma) <sub>2</sub>, (beta gamma)<sub<1</sub> (alpha)<sub>2</sub>), and/or (alpha)<sub>4</sub>. The electron micrographs show that the sulphide-binding serum component is a dumbbell-shaped molecule consisting of two globular subunits of 74 plus or minus 5 nm. It is a glycosylated molecule (non-haeme) that also possesses a protein moiety. Its absorbance peak shifts from 280 nm to 208 nm when it binds sulphide. This molecule moreover possesses unusual solubility properties suggesting that it may be a lipoprotein. It has a high zinc content and there is a 1:1 ratio between zinc and sulphide bound suggesting that zinc is the sulphide-binding site of this compound.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Haemoglobin structure and biochemical characteristics of the sulphide-binding component from the deep-sea clam <i>Calyptogena magnifica</i>","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":2000,"MonPub":null,"DateUpdate":"2016-04-21","DateCreate":"2004-10-11","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000166274500004","VABBcode":null,"OpenAcc":1},"refs":null,"anarec":{"AnaID":67003,"PubliDate":2000,"Pagination":"413-423","XtraPublOfAnaID":null,"ISBN":null,"Volume":"41","Issue":"4","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42348,"SerRR":"Cahiers de Biologie Marine. 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