Over het archief
Het OWA, het open archief van het Waterbouwkundig Laboratorium heeft tot doel alle vrij toegankelijke onderzoeksresultaten van dit instituut in digitale vorm aan te bieden. Op die manier wil het de zichtbaarheid, verspreiding en gebruik van deze onderzoeksresultaten, alsook de wetenschappelijke communicatie maximaal bevorderen.
Dit archief wordt uitgebouwd en beheerd volgens de principes van de Open Access Movement, en het daaruit ontstane Open Archives Initiative.
Basisinformatie over ‘Open Access to scholarly information'.
| one publication added to basket [280690] |
Phenoloxidase activity and thermostability of Cancer pagurus and Limulus polyphemus hemocyanin
Idakieva, K.; Raynova, Y.; Meersman, F.; Gielens, C. (2013). Phenoloxidase activity and thermostability of Cancer pagurus and Limulus polyphemus hemocyanin. Comp. Biochem. Physiol. (B Biochem. Mol. Biol.) 164(3): 201-209. https://dx.doi.org/10.1016/j.cbpb.2012.12.007
In: Comparative Biochemistry and Physiology. Part B. Biochemistry and Molecular Biology. Pergamon: Oxford. ISSN 1096-4959; e-ISSN 1879-1107, meer
|  |
| Trefwoorden |
Cancer pagurus Linnaeus, 1758 [WoRMS]; Limulus polyphemus (Linnaeus, 1758) [WoRMS]
Marien/Kust |
| Author keywords |
Hemocyanin; Cancer pagurus; Limulus polyphemus; Phenoloxidase activity;Thermal stability |
| Auteurs | | Top |
- Idakieva, K.
- Raynova, Y.
- Meersman, F., meer
- Gielens, C., meer
|
|
|
| Abstract |
The intrinsic and inducible o-diphenoloxidase (o-diPO) activity of Cancer pagurus hemocyanin (CpH) and Limulus polyphemus hemocyanin (LpH) were studied using catechol, l-Dopa and dopamine as substrates. The kinetic analysis shows that dopamine is a more specific substrate for CpH than catechol and l-Dopa (Km value of 0.01 mM for dopamine versus 0.67 mM for catechol, and 2.14 mM for l-Dopa), while kcat is highest for catechol (2.44 min− 1 versus 0.67 min− 1 for l-Dopa and 0.71 min− 1 for dopamine). On treatment with 4 mM sodium dodecyl sulfate (SDS) or by proteolysis the o-diPO activity of CpH increases about twofold. In contrast, native LpH shows no o-diPO activity, and exhibits only a slight activity after incubation with SDS. Neither CpH nor LpH show intrinsic mono-PO activity with l-tyrosine and tyramine as substrates. To explore the possible correlation between the degree of PO activity and protein stability of arthropod hemocyanins, the thermal stability of CpH and LpH was investigated by differential scanning calorimetry and Fourier transform infrared spectroscopy. CpH is found to be less thermostable (Tm ~ 80 °C), suggesting that the dicopper active sites are more accessible, thereby allowing the hemocyanin to show PO activity in the native state. The LpH, on the other hand, is more thermostable (Tm ~ 92 °C), suggesting the existence of a correlation between the thermal stability and the intrinsic PO activity of arthropod hemocyanins. |
IMIS is ontwikkeld en wordt gehost door het VLIZ.
