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15.
Mol Biol (Mosk) ; 21(4): 1117-23, 1987.
Article in Russian | MEDLINE | ID: mdl-3657782

ABSTRACT

The protein composition of the cytolytic factor (NKCF) secreted by natural killer cells was analyzed. Natural killer cells were isolated from spleens of nude rats and purified in the Percole gradient. SDS-PAAG analysis of NKCF revealed the presence of major proteins with an approximate molecular weight of 62-67 kDa. Biochemical properties of these proteins such as fractionation on a TSK-3000 SW gel filtration column, electrophoretical mobility in reduced conditions, enhanced cytolytical activity in the presence of Ca2+ demonstrate the similarity with the pore-forming protein--perforin. Apart from the major component, proteins with m. w. 42 kDa, 31-28 kDa, 17 kDa and 12-14 kDa were also found. It is possible that the Ca2+-independent cytolytical activity is bound to one of these minor protein components of NKCF.


Subject(s)
Killer Cells, Natural/analysis , Membrane Glycoproteins , Membrane Proteins/analysis , Proteins/analysis , Animals , Cytotoxicity, Immunologic , Electrophoresis, Polyacrylamide Gel , Humans , Killer Cells, Natural/immunology , Killer Factors, Yeast , L Cells , Membrane Proteins/immunology , Mice , Molecular Weight , Perforin , Pore Forming Cytotoxic Proteins , Proteins/immunology , Rats , Solubility
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