{"refrec":{"BRefID":12867,"RR":"<b>Pals, G.</b> (1978). De intracellulaire coeloom haemoglobine van de Annelide <i>Hetromastus filiformis</i>. <i>Interne verslagen Nederlands Instituut voor Onderzoek der Zee</i>, 1978(6). NIOZ: Texel.  42 pp.","BEntID":12867,"PublicFlag":1,"CheckedFlag":0,"wosflag":0,"vabbflag":0,"RefStringPartII":". <i>Interne verslagen Nederlands Instituut voor Onderzoek der Zee</i>, 1978(6). NIOZ: Texel.  42 pp.","DocTypID":13,"DocType":"Reports","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Pals, G.","OrigTitleTranslFlag":1,"Authorstringtrunc":"Pals, G.","Englishabstract":"The intracellular coelomic haemoglobin of <i>Heteromastus filiformis</i> was studied. The haemoglobin is heterogeneous on the basis of isoelectric point. The four main components have i.e.p 5,86; 6,13; 6,95; 7,15. The molecular weight is between 6.000 and 10.000 Daltons. The 0<sub>2</sub> affinity is high (P<sub>50</sub> ~ 9 N.m<sup>-2</sup> for whole and haemolysed coelomic fluid and ~ 3,3 N.m<sup>-2</sup> for stripped haemoglobin; 15°C, pH 7,4). The Bohr factor is -0,34. There is a distinct Root-effect at pH < 6. The Hill-plots show a downward crack near 50% saturation, with slight to marked cooperativity below 50% saturation and none to slight cooperativity above 50 %. An association-dissociation equilibrium is suggested. ATP has an effect on O<sub>2</sub>-binding, but there probably are rather modificators. The results are discussed in relation to the measured environmental parameters.","AbstractOtherLang":"De intracellulaire coeloom haemoglobine van <I>Heteromastus filiformis</I> werd onderzocht. De haemoglobine is heterogeen wat iso-elektrisch punt betreft. De vier belangrijkste componenten hebben i.e.p. 5,86; 6,13; 6,95; 7,15. Het molecuulgewicht ligt tussen 6.000 en 10.000 Daltons. De 0<sub>2</sub> affiniteit is hoog (P<sub>50</sub> ~ 9 N.m<sup>-2</sup> voor hele en gehaemolyseerde coeloomvloeistof en ~ 3,3 N.m<sup>-2</sup> voor gestripte haemoglobine; 15°C, pH 7,4). De Bohr factor is -0,34. Er is een duidelijk Root-effekt bij pH < 6. De Hill-plots vertonen een neerwaartse knik bij 50% verzadiging, met redelijke tot sterke cooperativitiet beneden 50% en geen tot zwakke boven 50 %. Er wordt een associatie-dissociatie evenwicht van de haemoglobine voorgesteld. ATP heeft invloed op de O<sub>2</sub>-binding, maar er zijn waarschijnlijk nog andere modifikators. De resultaten worden besproken met betrekking tot de gemeten milieu parameters","BibLvlCode":"MS","StandardTitle":"De intracellulaire coeloom haemoglobine van de Annelide <i>Hetromastus filiformis</i>","OrigTitleLangCode":"nl","OrigTitleLangCodeExtended":"dut","OrigTitleLangID":41,"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":null,"MonPub":1978,"DateUpdate":"2019-08-20","DateCreate":"2001-07-04","SecASFANote":null,"ConfID":null,"PeerRev":0,"VlizCoreFlag":1,"WoScode":null,"VABBcode":null,"OpenAcc":1},"refs":null,"anarec":null,"monrec":{"MonID":12867,"ISBN":null,"PubliDate":1978,"IssueDate":null,"Volume":"1978","Issue":"6","Pagination":"42","Place":"Texel","Edition":null,"BRefXtra":null,"BRefXtraRR":null,"SerID":5036,"SerRR":"Interne verslagen Nederlands Instituut voor Onderzoek der Zee. 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