Journal:

Article Title: M-Like Proteins of Streptococcus dysgalactiae

doi:

Figure Lengend Snippet: SDS-PAGE and Western blotting. (a) The affinity-purified GST fusion proteins coded by pGDEMA7 and pGDEMA8 clones derived from S. dysgalactiae strain 8215 were separated on an SDS-PAGE gel (8 to 25% polyacrylamide) (A) and blotted to an NC membrane. Binding of Fg by the recombinant proteins was tested by probing with 125I-Fg and visualized by exposing the strips to x-ray film (B). IgG binding by the recombinant proteins was probed with HRP-labelled human (C) and rabbit (D) IgG while HRP-labelled protein G was used to detect the bound unlabelled horse IgG (E). Lanes: 1, GST; 2, GDEMA7; 3, GDEMA8. (b) Human Fg in reducing sample buffer and Fab and Fc fragments of human IgG in nonreducing sample buffer were separated on a homogeneous SDS–12% PAGE gel (A), transferred to an NC membrane, and probed with 125I-GDEMA8 protein. The bound probe was detected by exposing the membrane to x-ray film (B). Lanes: 1, Fg (from the top: α-, β-, and γ-chains); 2, human IgG Fab fragment; 3, human IgG Fc fragment. Molecular mass markers (kDa) are indicated.

Article Snippet: Rabbit anti-sheep IgG-HRP was the product of Southern Biotechnology Associates, Inc., Birmingham, Ala.

Techniques: SDS Page, Western Blot, Affinity Purification, Clone Assay, Derivative Assay, Binding Assay, Recombinant