Structure of a dimeric fragment related to the lambda-type Bence-Jones protein: A preliminary study
Abstract A Bence-Jones protein, Rhe, isolated from the urine of a myeloma patient, has been crystallized. Immunological tests indicate that Rhe contains the constant region of a lambda-type light chain. Gel filtration and sodium dodecyl sulfate gel electrophoresis show that Rhe consists of two subunits, each about half the size of the light chain. Preliminary X-ray crystallographic results and density measurements show that Rhe possesses crystallographic 2-fold symmetry, indicating that the two subunits of Rhe are identical. This is the first report of evidence suggesting the possible occurrence in Bence-Jones protein of dinners comprised of solely the constant half of the light chain. Heavy-atom derivatives, possibly useful for a crystal structure analysis, have been prepared.