Light‐scattering spectroscopic study of polysaccharide protein conjugate

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

doi:10.1002/bip.360210804

Light‐scattering spectroscopic study of polysaccharide protein conjugate

A. Patkowski, W. Bujalowski, B. Chu, R. Schneerson, J. B. Robbins

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

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) × 10² Å, apparent radius of gyration r_g ∼ (5.4 ± 0.3) × 10² Å, apparent molecular weight M_w ∼ (3.5 ± 0.4) × 10⁶ g/mol, and a second virial coefficient A₂ ∼ (1.9 ± 0.3) × 10⁻⁴ cm³ mol/g². 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.

Original language	English (US)
Pages (from-to)	1503-1520
Number of pages	18
Journal	Biopolymers
Volume	21
Issue number	8
DOIs	https://doi.org/10.1002/bip.360210804
State	Published - Aug 1982
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Biomaterials
Organic Chemistry

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title = "Light‐scattering spectroscopic study of polysaccharide protein conjugate",

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 rh ∼ (6.2 ± 0.6) × 102 {\AA}, apparent radius of gyration rg ∼ (5.4 ± 0.3) × 102 {\AA}, apparent molecular weight Mw ∼ (3.5 ± 0.4) × 106 g/mol, and a second virial coefficient A2 ∼ (1.9 ± 0.3) × 10−4 cm3 mol/g2. 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.",

author = "A. Patkowski and W. Bujalowski and B. Chu and R. Schneerson and Robbins, {J. B.}",

year = "1982",

month = aug,

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T1 - Light‐scattering spectroscopic study of polysaccharide protein conjugate

AU - Patkowski, A.

AU - Bujalowski, W.

AU - Chu, B.

AU - Schneerson, R.

AU - Robbins, J. B.

PY - 1982/8

Y1 - 1982/8

N2 - 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 rh ∼ (6.2 ± 0.6) × 102 Å, apparent radius of gyration rg ∼ (5.4 ± 0.3) × 102 Å, apparent molecular weight Mw ∼ (3.5 ± 0.4) × 106 g/mol, and a second virial coefficient A2 ∼ (1.9 ± 0.3) × 10−4 cm3 mol/g2. 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.

AB - 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 rh ∼ (6.2 ± 0.6) × 102 Å, apparent radius of gyration rg ∼ (5.4 ± 0.3) × 102 Å, apparent molecular weight Mw ∼ (3.5 ± 0.4) × 106 g/mol, and a second virial coefficient A2 ∼ (1.9 ± 0.3) × 10−4 cm3 mol/g2. 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.

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Light‐scattering spectroscopic study of polysaccharide protein conjugate

Abstract

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