Abstract
The refractive indices of orthorhombic and monoclinic crystals of β-lactoglobulin have been measured by microscope interferometry and found to be 1.4536 ± 0.0015 and 1.4765 ± 0.0015 respectively, these values being for a particular orientation of the light electric vector relative to the crystal axes. Combining these values with data4 on the dry weight of protein per unit volume of crystals, the specific refraction increments of orthorhombic and monoclinic crystals are calculated to be 0.00196 ± 0.00003 and 0.00191 ± 0.00002 respectively. The values are in fairly good agreement with that of 0.00182 found8 for dilute solutions of β-lactoglobulin. This conclusion is not altered when the birefringence of the crystals, which has also been measured, is taken into account. Both types of crystal approximate in behaviour to uniaxial crystals with birefringence values of 0.00086 ± 0.00003 and about 0.0036 for orthorhombic and monoclinic crystals respectively.
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