Study of neutral proteinases of human tear samples using gels containing copolymerized substrates

M. Punyiczki, A. Berta, J. Tozser

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Abstract

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.

Original languageEnglish
Pages (from-to)115-124
Number of pages10
JournalClinical Chemistry and Enzymology Communications
Volume1
Issue number2
Publication statusPublished - Jan 1 1988

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ASJC Scopus subject areas

  • Clinical Biochemistry

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