Related Experiment Video
Updated: Aug 20, 2026
From a 2DE-Gel Spot to Protein Function: Lesson Learned From HS1 in Chronic Lymphocytic Leukemia
Published on: October 19, 2014
Serine proteinase inhibitor from lymphocytic leukemia cells. Properties and copurification with DNA
1Department of Cytophysiology, Medical Center of Postgraduate Education, Warsaw, Poland.
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.
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.
