Purification, characterization, and unfolding studies of arginine kinase from Antarctic krill.

The regulation of enzymatic activity and unfolding studies of arginine kinase (AK) from various invertebrates have been the focus of investigation. To gain insight into the structural and folding mechanisms of AK from Euphausia superba (ESAK), we purified ESAK from muscle properly. The enzyme behaved as a monomeric protein with a molecular mass of about 40kDa and had pH and temperature optima of 8.

Folding studies of arginine kinase from Euphausia superba using denaturants.

Arginine kinase (AK) is a key metabolic enzyme for maintaining energy balance in invertebrates and studies on AK from Euphausia superba might provide important insights into the metabolic enzymes in extreme climatic marine environments. A folding study of the AK from E. superba (ESAK) has not yet been reported.

Effects of osmolytes on Pelodiscus sinensis creatine kinase: a study on thermal denaturation and aggregation.

The protective effect of osmolytes on the thermal denaturation and aggregation of Pelodiscus sinensis muscle creatine kinase (PSCK) was investigated by a combination of spectroscopic methods and thermodynamic analysis. Our results demonstrated that the addition of osmolytes, such as glycine and proline, could prevent thermal denaturation and aggregation of PSCK in a concentration-dependent manner. When the concentration of glycine and proline increased in the denatured system, the relative activation was significantly enhanced; meanwhile, the aggregation of PSCK during thermal denaturation was decreased.