CHROMATOGRAPHIC PROFILES OF CYANOGEN-BROMIDE FRAGMENTS OF UNREDUCED HUMAN SERUM-ALBUMIN ON IMMOBILIZED CIBACRON BLUE F3G-A

The elution profiles of cyanogen bromide fragments A (299-585), B (1-1 23), C (124-298) and D (1-298) of unreduced human serum albumin (HSA) on Cibacron Blue F3G-A immobilized on Sepharose CL-6B are reported. Th e binding properties of fragments C and D are similar to those of HSA, whereas fragment A shows a slightly lower retention time. Fragment B, in contrast, does not interact with the dye. The different chromatogr aphic behaviour of fragments B and C allows their fast separation by c ombined use of gel permeation and dye-protein affinity chromatography.