Purification and partial characterization of Arginine kinase from muscle tissue of shrimp, Littopenaeus vannamei

The arginine kinase was purified from muscle tissue of the shrimp, Littopenaeus vannamei. The crude extract was treated with CM-cellulose in a batch procedure. Fractionation of arginine kinase was performed by SephadexG-100 chromatography and followed by DEAE-cellulose 32 ion-exchange chromatography. The molecular weight of it was about 40 ku, as judged by SDS-polyacrylamide-gel electrophoresis. The enzyme remained stable at 25-55℃ within 60 min and inactivated at higher temperature (65℃). The activity of purified shrimp arginine kinase was remained stable in the range of pH 6.0-8.0. Treated with 10 mmol·L^-1 arginine, NaCl, KCl, MgCl₂, the enzyme activity significantly increased. However, the enzyme activity was obviously inhibited by its substrate analogs such as spermine, amino guanidine, CuCl₂, MnCl₂.