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Light‐scattering spectroscopic study of polysaccharide protein conjugate
Author(s) -
Patkowski A.,
Bujalowski W.,
Chu B.,
Schneerson R.,
Robbins J. B.
Publication year - 1982
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360210804
Subject(s) - chemistry , conjugate , radius of gyration , bovine serum albumin , fractionation , gel permeation chromatography , hydrodynamic radius , chromatography , virial coefficient , analytical chemistry (journal) , polymer , organic chemistry , copolymer , mathematical analysis , physics , mathematics , quantum mechanics
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.