Serine proteinase inhibitor from lymphocytic leukemia cells. Properties and copurification with DNA.
A trypsin inhibitor was isolated from mouse lymphocytic leukemia L 1210 cells by ammonium sulphate precipitation and preparative isoelectric focusing. A 39-fold purification was attained. The inhibitor is a protein since its activity is destroyed by pronase and it binds to insolubilized trypsin. Two main forms of the inhibitor were found of pH 4.8 and 5.3. The inhibitor is copurified with DNA, although neither DNase II nor RNase A change its activity.
Hoser
G
G
Department of Cytophysiology, Medical Center of Postgraduate Education, Warsaw, Poland.
Kawiak
J
J
D000645:Ammonium Sulfate; D000818:Animals; D002846:Chromatography, Affinity; D004247:DNA / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D005590:Fractional Precipitation; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007939:Leukemia L1210 / Q000378:metabolism*; D051379:Mice; D008970:Molecular Weight; D011506:Proteins / Q000302:isolation & purification* / Q000378:metabolism; D015842:Serine Proteinase Inhibitors; D013056:Spectrophotometry, Ultraviolet; D014357:Trypsin / Q000378:metabolism; D014361:Trypsin Inhibitors
D011506:Proteins; D015842:Serine Proteinase Inhibitors; D014361:Trypsin Inhibitors; D004247:DNA; D014357:Trypsin; D000645:Ammonium Sulfate