Structure of a dimeric fragment related to the lambda-type Bence-Jones protein: A preliminary study

Published on Aug 1, 1974in Journal of Molecular Biology5.067
· DOI :10.1016/0022-2836(74)90100-4
Bi-Cheng Wang48
Estimated H-index: 48
Martin Sax21
Estimated H-index: 21
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.
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