Comparison of proteins synthesized by two different isolates of Anaplasma marginale

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Abstract
The initial definition of proteins synthesized by 2 isolates of A. marginale is presented. Bovine erythrocytes infected with A. marginale were radioactively labeled with [35S]methionine or a 3H-amino acid mixture during short-term in vitro culture. The labeled proteins were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This technique revealed protein bands of various MW from < 14,000 to > 200,000. The bands observed represented A. marginale proteins because uninfected erythrocytes from the same animal did not incorporate radioisotope during identical culture conditions, and the incorporation of radioisotope into proteins during culture of infected erythrocytes was inhibited by tetracycline but not by cycloheximide. The radioactive protein profiles of 2 different isolates of A. marginale, from Washington and Florida [USA], were compared by 2-dimensional gel electrophoresis; .apprx. 200 proteins were resolved in each case. Several proteins differed in position when the 2-dimensional gel maps were compared compared, indicating variations in protein structure between the A. marginale isolates.