Analysis of aggregates of human immunoglobulin G using size-exclusion chromatography, static and dynamic light scattering

被引：76

作者：

Ahrer, K

Buchacher, A

Iberer, G

Josic, D

Jungbauer, A

机构：

[1] Univ Nat Resources & Appl Sci, Inst Appl Microbiol, A-1190 Vienna, Austria

[2] Octapharma Pharmazeut, A-1100 Vienna, Austria

来源：

JOURNAL OF CHROMATOGRAPHY A | 2003年 / 1009卷 / 1-2期

关键词：

hydrodynamic radius; light-scattering detection; detection; LC; immunoglobulins; proteins;

D O I：

10.1016/S0021-9673(03)00433-3

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Large aggregates (M-r: 10(6)-10(7) g/mol) of human immunoglobulins are present in extremely small concentrations in IgG preparations (<0.1%). Traces of large protein aggregates cannot be determined by conventional size-exclusion chromatography (SEC) using UV detection due to limitations in sensitivity. The conventional analysis of IgG by SEC is limited to dimers and oligomers. Using light scattering it is possible to determine significant differences concerning the aggregate composition and the extent of protein aggregation in samples of different process steps. Two different pilot preparations were analyzed by SEC with UV and static light scattering detection and compared to dynamic light scattering in the batch mode. The change of large aggregates could be monitored and data were corroborated by dynamic light scattering. (C) 2003 Elsevier B.V. All rights reserved.

引用

页码：89 / 96

页数：8

共 23 条

[1] PHOTON-CORRELATION SPECTROSCOPY AND LIGHT-SCATTERING OF EYE LENS PROTEINS AT HIGH-CONCENTRATIONS [J].