Abstract
Methods are given for the isolation and crystallization of bovine β-lactoglobulin C. Properties of this new variant are compared with those of the A and B variants. There are differences in crystallization behaviour. The nitrogen contents and monomer molecular weights of the three variants are similar. The C variant shows little or no tendency to associate at pH 4.7 and low temperature, resembling the B variant and not the A variant. The laevorotation of C at pH 5.2 is slightly greater than that of the A or B variant but a o and b o are similar for all three variants. The ultraviolet absorption spectrum of C differs slightly from that of A or B. Optical rotatory dispersion and sedimentation studies indicate different stabilities for A, B and C and different tendencies for them to dissociate. The order of stability and dissociation are pH dependent. The three variants exhibit similar immunological behaviour.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure
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