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Inhibition of the cathepsin B like proteinase by a low molecular weight cysteine-proteinase inhibitor from ascitic fluid and plasma alpha 2 macroglobulin

Pagano, M ; Keppler, D ; Fumeron-Dalet, V ; Engler, R

Biochemistry and cell biology, 1986-12, Vol.64 (12), p.1218-1225 [Periódico revisado por pares]

Canada

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  • Título:
    Inhibition of the cathepsin B like proteinase by a low molecular weight cysteine-proteinase inhibitor from ascitic fluid and plasma alpha 2 macroglobulin
  • Autor: Pagano, M ; Keppler, D ; Fumeron-Dalet, V ; Engler, R
  • Assuntos: alpha-Macroglobulins - metabolism ; Ascites - enzymology ; Cathepsin B - antagonists & inhibitors ; Cathepsin B - metabolism ; Cysteine Proteinase Inhibitors ; Female ; Humans ; Kinetics ; Molecular Weight ; Ovarian Neoplasms - metabolism ; Protease Inhibitors - metabolism
  • É parte de: Biochemistry and cell biology, 1986-12, Vol.64 (12), p.1218-1225
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
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  • Descrição: The cathepsin B like proteinase present in ascitic fluid of a patient with neoplasia has been purified and characterized after pepsin activation. From this fluid we have prepared the low molecular weight (LMW) cysteine-proteinase inhibitors. Three major inhibitor forms were found with isoelectric points of 7.4, 5.4, and 5.1, respectively. The interaction of the enzyme with the former inhibitor was studied because this inhibitor was the most abundant. The Ki value was found to be 4.3 X 10(-8) M. Two molecules of this proteinase were bound by one molecule of plasma alpha 2 macroglobulin (alpha 2M). The LMW inhibitor was able to bind to the enzyme entrapped in alpha 2M and reduced its endopeptidase activity on benzyloxycarbonyl-L-phenylalanyl-L-arginine-4-methyl-7-coumarylamide. These results may have a physiological significance in the regulation of the enzyme which, among other extracellular hydrolases, probably plays an important role in tumor invasion.
  • Editor: Canada
  • Idioma: Inglês

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