[Proteinase-inhibitors and enzyme-active proteins from fish eggs. Fibrinagarelectrophoretic and immunoelectrophoretic studies (author's transl)].

Saline extracts from eggs and homogenized spermaplasma from 2 fresh water fishes and 2 sea-fishes were investigated using fibrin-agar-electrophoresis and the 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. Fresh water fishes contained more inhibitors than sea-fishes. 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 Salmo gairdneri. The separation of pseudo- and euglobuline fractions permitted a 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. By means of cross reactions it could be demonstrated the nonspecificity of several proteins in respect to species, genus and sex. This concernes also some aspects of immunesera absorptions with heterologous protein mixtures. Cross reactions with proteinase-inhibitors couldn't be detected, suggesting that they are genus-specific. This is also confirmed by their variable number and inhibition-spectra in extracts of different origin.