Characterization of group A streptococcal T-12 protein purified by ion-exchange column chromatography.

The aim of the present study was to describe the physicochemical characteristics of streptococcal T antigen. T protein isolated from Streptococcus pyogenes type 12 (R53/1077, Colindale) and purified by ion-exchange column chromatography resulted in a preparation that was homogeneous when tested electrophoretically (in two systems, in presence and in absence of sodium dodecyl sulfate) and by gel filtration on Sephadex G-100. The purified T antigen was resistant to enzymatic degradation by trypsin and pepsin. It formed a single precipitin line with standard T-12 antiserum and was not contaminated with group A carbohydrate and M protein. The molecular weight of protein T, determined by means of polyacrylamide gel electrophoresis and calculated from its amino acid composition, was about 39,000. The molecular weight of this protein, determined by means of high-speed sedimentation equilibrium, ranged between 80,000 and 120,000. Glutamic and asparatic acids, lysine, alanine, and leucine were the predominant amino acids.