Neutral proteinases in human tear samples were investigated with radial diffusion, agarose gel and SDS-polyacrylamide gel electrophosesis using gels containing casein in the presence and absence of plasminogen as copolymerixed substrates. By radial diffusion plasminogen activator activity was detected even in normal tears, but no plasminogen-independent proteolytic activity was found. However, in some pathological human tears plasminogen-independent proteolysis also occurred. Using agarose gel electrophoresis two caseinolytic zones, which were resistant against the proteinase inhibitors, could be detected. These lytic zones are at least partially the result of an artefact due to the high lysozyme content of tears. By SDS-polyacrylamide gel electrophoresis plasminogen independent proteinases of higher molecular mass were detected only in certain diseases. However, both normal and pathological human tears contained closely spaced doublet bands of plasminogen activator /Mr 55-58 and 48-53 kDa/ suggesting that plasminogen activator in tear is a urokinase-type.
|Number of pages||10|
|Journal||Clinical Chemistry and Enzymology Communications|
|Publication status||Published - Jan 1 1988|
ASJC Scopus subject areas
- Clinical Biochemistry