Bence-Jones proteins

Abstract

Bence-Jones proteins from 5 cases of myelomatosis were examined and found to differ in their properties. The most marked variation occurred with 2 specimens that did not re-dissolve in boiling salt solutions. In the presence of 40% alcohol, all the Bence-Jones proteins coagulated when warmed and redissolyed when boiled. Serum proteins, however, behaved similarly in the presence of 40% alcohol. The author believes this effect is due to a shift in the apparent isoelectric point with the resulting formation of more soluble salts, rather than due to a solvent action of the alcohol.