Isolation and immunological characterization of three highly purified serine proteinases from Antarctic krill ( Euphausia superba )

摘要: Three individual serine proteinases (I, II, III) originating from Antarctic krill (E. superba) were separated and highly purified using a combination of affinity high resolution ion exchange chromatography. Each enzyme showed single protein band (30 000 Daltons) in sodium dodecyl sulphate polyacrylamide gradient gel electrophoresis indicating purity identical molecular weights. Moreover, each demonstrated one immunoprecipitate on crossed immunoelectrophoresis (two-dimensional agarose electrophoresis) polyclonal rabbit antibodies which confirmed the enzymes. A mixture three enzymes revealed two immunoprecipitates, not or should have been case for non-identical immunological properties. Double immunodiffusion test according to Ouchterlony exhibited identity between II III. Enzyme I only partial with II/III. These findings correlated well biochemical data proteinases. is able liberate free amino acids polypeptides comparison III (classical true endopeptidases), do not. We suggest that these unique properties also their counterpart expressed as other antigenic determinants structure.