Aggregation of Human Immunoglobulin G upon Freezing.

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Abstract
Investigation of the aggregation of normal and myeloma immunoglobulins when frozen revealed a correlation between the percentage of formed aggregates and storage period in the cold. No correlation was found between the percentage of formed aggregate and protein concentration in the interval 0.2-1.4 g/100 ml. The amount of aggregates formed varied between 26 and 42% for 4 different normal IgG''s. The amount of aggregate of the order of 10 S varied between 22 and 33% and the amount of aggregate of the order of 12 S between 4 and 10%. Traces of precipitate occurred in 3 preparations. The amount of aggregate formed varied between 13 and 42% for 7 myeloma IgG. The amount of aggregate with the order of 10 S varied between 13 and 32% and the amount ot aggregate with an order of 12 S between 0 and 10%. Traces of precipitate occurred in 3 preparations. A certain correlation was found between the electro-phoretic mobility of the myeloma IgG and the percentage of formed aggregate but not between the percentage of formed aggregate and type of light chain, Gm-type, or sedimentation constant. 7 S molecules separated from formed aggregates could form aggregates to the same extent as the original population of IgG molecules.

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