Comparative characterization of the hemocyanin-derived phenol oxidase activity from spiders inhabiting different thermal habitats

Cubillos, Claudio; Caceres, Juan Carlos; Villablanca, Cristopher; Barriga, Andres; Cabrera, Ricardo; Veloso, Claudio

Abstract

Enzymes adapted to cold temperatures are commonly characterized for having higher Michaelis-Menten constants (K-M) values and lower optimum and denaturation temperature, when compared to other meso or thermophilic enzymes. Phenoloxidase (PO) enzymes are ubiquitous in nature, however, they have not been reported in spiders. It is the oxygen carrier protein hemocyanin (He), found at high concentrations in their hemolymph, which displays an inducible PO activity. Hence, we hypothesize that Hc-derived PO activity could show features of cold adaptation in alpine species. We analyzed the He from two species of Theraphosidae from different thermal environments: Euathlus condorito (2400 m a.s.l.) and Grammostola rosea (500 m a.s.l.). He was purified from the hemolymph of both spiders and was characterized by identifying subunit composition and measuring the sodium dodecyl sulfate (SDS)-induced PO activity. The high-altitude spider He showed higher PO activity under all conditions and higher apparent Michaelis-Menten constant. Moreover, the optimum temperature for PO activity was lower for E. condorito Hc. These findings suggest a potential adaptation at the level of Hc-derived PO activity in Euathlus condorito, giving insights on possible mechanisms used by this mygalomorph spider to occupy extremes and variable thermal environments.

Más información

Título según WOS: Comparative characterization of the hemocyanin-derived phenol oxidase activity from spiders inhabiting different thermal habitats
Título de la Revista: COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
Volumen: 253
Editorial: Elsevier Science Inc.
Fecha de publicación: 2021
DOI:

10.1016/j.cbpb.2020.110548

Notas: ISI