6533b852fe1ef96bd12aabfb
RESEARCH PRODUCT
Identification, structure, and properties of hemocyanins from Diplopod myriapoda.
Elmar JaenickeThorsten BurmesterHeinz DeckerJürgen MarklWolfgang Gebauersubject
MaleProtein Conformationmedicine.medical_treatmentBlotting WesternMyriapodachemical and pharmacologic phenomenaCooperativityCross Reactionscomplex mixturesBiochemistryEpitopesHemolymphmedicineAnimalsMolecular BiologyArthropodsbiologyhemic and immune systemsHemocyaninCell BiologyAnatomybiology.organism_classificationSpirostreptusOxygenBiochemistrySpectrophotometryHemocyaninsElectrophoresis Polyacrylamide GelFemaleArthropodSpirostreptidaeScutigera coleoptrataProtein Bindingdescription
Hemocyanins are copper-containing, respiratory proteins that occur in the hemolymph of many arthropod species. Here we report for the first time the presence of hemocyanins in the diplopod Myriapoda, demonstrating that these proteins are more widespread among the Arthropoda than previously thought. The hemocyanin of Spirostreptus sp. (Diplopoda: Spirostreptidae) is composed of two immunologically distinct subunits in the 75-kDa range that are most likely arranged in a 36-mer (6 x 6) native molecule. It has a high oxygen affinity (P(50) = 4.7 torr) but low cooperativity (h = 1.3 +/- 0.2). Spirostreptus hemocyanin is structurally similar to the single known hemocyanin from the myriapod taxon, Scutigera coleoptrata (Chilopoda), indicating a rather conservative architecture of the myriapod hemocyanins. Western blotting demonstrates shared epitopes of Spirostreptus hemocyanin with both chelicerate and crustacean hemocyanins, confirming its identity as an arthropod hemocyanin.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1999-10-03 | The Journal of biological chemistry |