Low molecular weight inhibitors of cathepsins B, H and T in human serum, synovial fluid and CSF

When human plasma was chromatographed on a Sephadex G-75 column, cathepsin B inhibitors with molecular weights of 80,000 and 13,000 were eluted. The high molecular weight peak (TPI-H) contained α-thiol proteinase inhibitor and haptoglobin, both of which inhibited cathepsins B and H. The low molecula...

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Veröffentlicht in:Biochemical and biophysical research communications 1982-10, Vol.108 (4), p.1581-1587
Hauptverfasser: Lenney, James F., Liao, John Rose, Sugg, Sonia L., Gopalakrishnan, Vijaya, Wong, Henry C.H., Ouye, Keith H., Chan, Paul W.H.
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Sprache:eng
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Zusammenfassung:When human plasma was chromatographed on a Sephadex G-75 column, cathepsin B inhibitors with molecular weights of 80,000 and 13,000 were eluted. The high molecular weight peak (TPI-H) contained α-thiol proteinase inhibitor and haptoglobin, both of which inhibited cathepsins B and H. The low molecular weight peak (TPI-L) inhibited cathepsins B, H and T, but had little or no activity against papain, ficin or bromelain. TPI-L from plasma contained two molecular forms of inhibitor, while TPI-L from pooled serum samples contained nine. Serum TPI-L was found to be different from the low molecular weight inhibitors present in lung and many other organs. When rheumatoid synovial fluid was analyzed by gel filtration, the eluate contained TPI-H and TPI-L. Human cerebrospinal fluid eluates contained TPI-L, but not TPI-H.
ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(82)80088-0