PROTEINASE-INHIBITORS AND ENZYME-ACTIVE PROTEINS FROM FISH EGGS FIBRIN-AGAR ELECTROPHORETIC AND IMMUNOELECTROPHORETIC STUDIES

  • 1 January 1975
    • journal article
    • research article
    • Vol. 150  (2) , 161-174
Abstract
Saline extracts from eggs and homogenized sperm plasma from 2 freshwater [Salmo gairdneri and Perca fluviatilis] and 2 sea water fish [Clupea harengus and Gadus callaris] were investigated using fibrin agar electrophoresis and immunoelectrophoretic analysis. Many polyvalent proteinase-inhibitors with different inhibition spectra, lipoproteins and esterase active proteins which split .beta.-naphthylacetate as substrate were detected and designated according to a proposed nomenclature. Freshwater fish contained more inhibitors than sea water fish. The proteinase-inhibitor PI-Sg3 antigen-antibody complex was esterase active; the active complex designated PI-Sg4 could not yet be exactly coordinated in respect to another proteinase-inhibitor from S. gairdneri. The separation of pseudo- and euglobulin fractions permitted significant concentration of proteinase-inhibitors and the elimination of large parts of strong antigenic proteins. A good antiserum could be prepared which showed 3-5 precipitation lines against proteinase-inhibitors from trout eggs. Using cross reactions the nonspecificity of several proteins with respect to species, genus and sex was shown, as well as some aspects of immune sera absorptions with heterologous protein mixtures. Cross reactions with proteinase-inhibitors could not be detected, suggesting that they are genus-specific. This is also confirmed by their variable number and inhibition spectra in extracts of different origin.