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Bence-Jones Proteins and Light Chains of Immunoglobulins

V. X-RAY CRYSTALLOGRAPHIC INVESTIGATION OF THE AMINO-TERMINAL HALF OF A BENCE-JONES PROTEIN

From the ¹ From the University of Tennessee Memorial Research Center and Hospital, Knoxville, Tennessee 37920
² From the Biology Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37830

The ability to cleave specifically a human type Bence-Jones protein (LEN) into its amino-terminal (variant) half and carboxyl-terminal (constant) half made possible the preparation and isolation of the variant half in quantities sufficient for immunochemical and physicochemical studies on the properties of the variant half of a light polypeptide chain. The variant half (V_l) was readily crystallized in a form suitable for x-ray diffraction studies. The V_l crystals were monoclinic with space group P2; the unit cell dimensions from 13° precession photographs were a = 65.6 ± 0.1 A, b = 37.9 ± 0.1 A, c = 43.5 ± 0.1 A, ß = 90.0 ± 0.2°. The number of V_l molecules (mol wt 11,500) per asymmetric unit was calculated to be 2 and the number of molecules per unit cell was 4.

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