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A membrane‐associated cysteine protease inhibitor from murine hepatoma
Author(s) -
Moin Kamiar,
Emmert Leslie T.,
Sloane Bonnie F.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80789-j
Subject(s) - polyclonal antibodies , protease inhibitor (pharmacology) , isoelectric point , microbiology and biotechnology , isoelectric focusing , chemistry , cysteine , cysteine protease , biochemistry , monoclonal antibody , cysteine proteinase inhibitors , antibody , protease , cystatin , biology , enzyme , cystatin c , virology , virus , apoptosis , programmed cell death , viral load , antiretroviral therapy , caspase , immunology , renal function
A cysteine protease inhibitor was purified from total membrane fractions of an invasive murine hepatoma, Hepa cl 9. On gel filtration under non‐reducing conditions the purified inhibitor was eluted in a single peak of M 1 10–15 kDa, but resolved as two bands at 14 and 70 kDa on SDS‐PAGE under reducing conditions. By isoelectric focusing, the inhibitor ran at an isoelectric point of 4.75. Immunoblotting studies using the enhanced chemiluminescence technique indicated no crossreactivity with monoclonal antibodies to stefin B and cystatin C or with a polyclonal antibody to low M ??? kininogen. In contrast, the 14 kDa and 70 kDa bands both crossreacted with a polyclonal antibody to stefin A, suggesting that the cysteine protease inhibitor associated with Hepa cl 9 membranes may be a modified form of stefin A.