PMID: 6722217Mar 1, 1984

Study of conformational changes in immunoglobulin M using the method of differential spectroscopy

Biokhimii︠a︡
E D Kaverzneva, A I Chukhrova

Abstract

Using differential and solvent-perturbation spectrophotometry, the nature of conformational changes in immunoglobulin M (IgM) in different regimens was investigated. The quantities of tryptophan and tyrosine chromophores exposed on the surface of the molecule and screened, were evaluated. The changes in pH (7.8----2.0) of the surrounding medium and splitting of carbohydrate groups from IgM were shown to cause opposite effects, i. e., a "blue shift" of the spectrum and exposure of new chromophores by acidification, and a "red shift" and screening of chromophores by splitting of carbohydrate groups. The experimental results agree well with the previously made assumption on the differences in the spatial conformational changes in the IgM molecule under effects of pH of the surrounding medium and the loss of carbohydrate groups. Analysis of the spectral characteristics of some free Fab- and (Fc)5-fragments derived from the IgM molecules allowed a specification of the changes occurring in different parts of the whole molecule. The main conformational changes after acidification occur in the (Fc)5-fragment responsible for the effector function of IgM.

Related Concepts

Tryptophan
Acidification - ActCode
Immunoglobulin M Measurement
Fab Immunoglobulins
Immunoglobulin M
IgM2
Spectrophotometry, Analyte Not Elsewhere Specified in CPT
Protein Conformation
Spectrophotometry, Ultraviolet
PMS-Tryptophan

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