The finding that mactinin is detected by Western blotting of samples run under reducing conditions without immunoaffinity purification seems to confirm this.

Protein A in various recombinant forms has been used for decades to bind and purify a wide range of antibodies by immunoaffinity chromatography.

After purification by immunoaffinity chromatography and gel filtration, the deglycosylated sCD2 readily crystallized.

Immunoaffinity chromatography uses the specific binding of an antibody to the target protein to selectively purify the protein.

Sequential immunoaffinity columns were used to purify β-tubulin classes II and III with their associated α-tubulins as described previously [ 12 ] .

A Hybridoma Laboratory provided for the development of monoclonal antibodis for analyses (ELISA) and immunoaffinity chromatography.

These polypeptides comigrated with the 63K and 240K polypeptides of the cGMP-gated channel complex isolated on an anti-channel immunoaffinity column (Fig. 4 (left), lane c).

Because mactinin is a very small fraction of the total protein content (more than 50 μg/10 μl) of the fluid, immunoaffinity purification of mactinin was performed before Western blotting.

The protein levels in lavage fluid from arthritic joints in this model are low enough to allow direct testing by Western blot analysis without immunoaffinity purification, as was needed with the human aspirates.

FIG. 4 Purification of the cGMP-gated channel complex by calmodulin and immunoaffinity chromatography and identification of the 240K channel-associated protein as a major calmodulin-binding polypeptide of ROS membranes.

CD44 glycoprotein was purified from a monocyte-rich preparation of peripheral blood mononuclear leukocytes by immunoaffinity chromatography using monoclonal antibody raised against CD44, NIH44-1 (ref. 39), and applied at 1ng per well (estimated by silver staining).