Worsham L M, Tucker M, Ernst-Fonberg M L
Department of Biochemistry, Quillen-Dishner College of Medicine, East Tennessee State University, Johnson City 37614.
Biochim Biophys Acta. 1990 Apr 2;1043(2):198-202. doi: 10.1016/0005-2760(90)90296-a.
Acyl carrier proteins (ACPs) from Escherichia coli and Euglena were analyzed on Western blots using rabbit antibodies raised against E. coli ACP. Euglena ACP, unlike that from E. coli, behaves upon electrophoresis under denaturing conditions as its size would predict. Oligomeric forms of both ACPs were evident on Western blots, but the bacterial ACP had more tendency to aggregate. That the oligomeric forms were not due to impurities was shown by their regeneration from low-Mr protein, reaction with antibodies isolated from low-Mr protein, and by molecular weight determination of the ACP by low-angle laser light scattering.
