Intrinsically stable IgG aggregates.

Abstract:

:Measurement of the absorbance due to light scattering at 40 nm proved to be a simple and reliable way of assessing the extent of aggregation in heat-treated IgG solutions. Using this technique the rate of aggregation was demonstrated to be markedly temperature dependent with a sharp inflexion in the curve close to 63 degrees C. During heating at 63 degrees C the concentration of unaggregated IgG fell in a manner consistent with a first-order process and the mean size of the IgG aggregates increased with time. IgG aggregates could be selectively removed from heat-treated IgG solutions and concentrated by precipitation with 3.5% polyethylene glycol without altering their size distribution. Furthermore, and in contrast with a previous report, the IgG aggregates examined in this study were remarkably stable in the absence of any other protein such as serum albumin. In consequence, several important practical recommendations concerning the production of heat-aggregated IgG for use in immune complex assays are made.

journal_name

J Immunol Methods

authors

McCarthy D,Goddard DH,Pell BK,Holborow EJ

doi

10.1016/0022-1759(81)90274-x

subject

Has Abstract

pub_date

1981-01-01 00:00:00

pages

63-74

issue

1

eissn

0022-1759

issn

1872-7905

pii

0022-1759(81)90274-X

journal_volume

41

pub_type

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