Abstract
The EDTA extractable protein (EEP) can be prepared from the bovine lens using sonication; however, urea washing of the membrane fraction was essential in decreasing the non-specific binding of the crystallins to the EEP fraction. Both the 32 and the 35 kilodalton (kD) proteins from EEP were shown to be glycoconjugates using periodate labelling. The EEP from the lens bound a variety of lectins at both 32 and 35 kD. The binding of the lectins suggested that EEP is composed of proteins having galactose or N-acetylgalactosamine groups as well as fucose residues. The glycosylation of EEP adds another possible regulatory step for the control of these calcium binding proteins in the lens.
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