Purification And Characterization Of Arginine Kinase From Locust

L-Arginine kinase (AK; ATP: L-arginine N-phosphotransferase; EC 2.7.3.3) is a member of what appears to be a highly conserved family of phosphotransferases which reversibly catalyze the transfer of phosphate from phospoarginine to ADP yielding ATP, so it buffers cellular ATP levels. AK only exists in invertebrates, and phospoarginine and its biosynthetic pathway are totally different from those in mammalian host tissues, points out this AK as a possible target for the control of insect pests. AK was purified from the leg muscle of the locust Migratoria manilensis. In the paper, purification and characterization were studied so that we could provide clues to the control of insect pests, ultimately. By the investigation, the following results were achieved:1. Separation and purification of AK Leg muscle of locust was homogenized in ice, then centrifuged and the supernatant was purified by Sephacryl S-200 HR gel filtration chromatography; purification fold was 3.4 and recovery was 94%. This chromatography step was very efficient, for the specific activity was highly increased and great deal amount of activity was maintained. Further purification was achieved by DEAE Sepharose CL-6B Fast Flow anion exchange chromatography; ultimately AK was purified up to s 11.9 with a recovery of 80%. SDS-PAGE and Native-PAGE of AK indicated...