IDENTIFICATION OF A CA2-DEPENDENT AGAROSE-BINDING PROTEIN IN CHICKEN SERUM()

A Ca2+-dependent agarose-binding protein was purified from chicken ser um by affinity chromatography on SeaKem agarose gels followed by gel f iltration on Sephacryl S-300. Purified protein was eluted in a symmetr ical peak at the position of molecular weight of 146,000. In sodium do decyl sulfate-polyacrylamide gel electrophoresis, it was resolved into a single protein band with a molecular weight of 39,000 under nonredu cing and of 41,000 under reducing conditions. Thus, the agarose-bindin g protein is suggested to be composed of noncovalently-associated iden tical subunits which contain intrachain disulfide bonds.