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Peptide Mapping of Actin by limited Proteolysis and Immunoblotting Using an Anti-amoeba-actin Monoclonal Antibody as a Probe

Molecules and Cells 1990년 1권 1호 p.61 ~ 65
 ( Ahn Tae-In ) - Seoul National University Department of Biology Education

 ( Jean Kwang-Woo ) - Seoul National University Department of Biology Education


Cytosolic actin (43 kDa) of Amoeba proteus purified from preparative SDS-polyacrylamide gels by electroelution was analyzed and compared with actins from other sources using a monoclonal antibody as a probe. In the immunoblot of 2D-PAGE, actins of various sources showed a typical pattern of fragmentation by limited proteolysis with chymotrypsin. But the tryptic peptide pattern of amoeba actin was different from that of other actins. The variability of amoeba actin was most prominent by digesting with V8 protease. By the analysis and comparison of the actin sequences, the epitope of the amoeba actin was postulated to be in the region between amino acid residues 150 and 300.


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