Light-scattering spectroscopic study of polysaccharide protein conjugate

✍ Scribed by A. Patkowski; W. Bujalowski; B. Chu; R. Schneerson; J. B. Robbins

• Publisher: Wiley (John Wiley & Sons)
• Year: 1982
• Tongue: English
• Weight: 805 KB
• Volume: 21
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360210804

✦ Synopsis

Abstract

By combining gel permeation chromatography (GPC) and light‐scattering spectroscopy, including photon correlation and angular distribution of absolute scattered intensity, we were able to characterize immunologically active Haemophilus influenzae type b polysaccharide (HIB Ps) bovine serum albumin (BSA) conjugates in terms of equivalent hydrodynamic radius r~h~ ∼ (6.2 ± 0.6) × 10^2^ Å, apparent radius of gyration r~g~ ∼ (5.4 ± 0.3) × 10^2^ Å, apparent molecular weight M~w~ ∼ (3.5 ± 0.4) × 10^6^ g/mol, and a second virial coefficient A~2~ ∼ (1.9 ± 0.3) × 10^−4^ cm^3^ mol/g^2^. We could study the effects of each of the processes in the conjugate formation according to the following procedure: BSA (dialysis, modification, fractionation) + HIB Ps → HIB Ps/BSA conjugate (conjugate formation, fractionation). Narrow distributions of HIB Ps BSA conjugate formation can be achieved using fractionated BSA.