Abstract
Secreted proteins and other components of the Uromyces appendiculatus urediospore germling extracellular matrix were fractionated by a scheme employing a hydrophobic-silanized, fumed silica matrix. Two fractions of secreted proteins were obtained by this procedure. One fraction was adsorbed by hydrophobic interactions from germination water filtrate. The second group of components, apparently less hydrophobic in character and left behind in solution, was subsequently fractionated by anion-exchange chromatography. The total protein and glycoprotein profiles of several fractions were compared after sodium dodecyl sulfate Polyacrylamide gel electrophoresis. Batch extraction of putative adhesion proteins by silanized fumed silica matrices is proposed as a one-step procedure for extracellular matrix antigen preparation.