PMID: 6403551Feb 1, 1983Paper

Intracellular distribution and degradation of immunoglobulin G and immunoglobulin G fragments injected into HeLa cells

The Journal of Cell Biology
T McGarryM Rechsteiner

Abstract

Intact rabbit immunoglobulin G molecules (IgGs) and their papain or pepsin fragments were radio-iodinated and injected into HeLa cells. Whole IgGs, Fab2, and Fc fragments were degraded with half-lives of 60-90 h, whereas half-lives of Fab fragments were 110 h. These results indicate that proteolytic cleavage in the hinge region of the IgG molecule is not the rate-limiting step in its intracellular degradation. The hingeless human myeloma protein, Mcg, was degraded at the same rate as bulk human IgG, providing further evidence that the proteolytically susceptible hinge region is not important for intracellular degradation of IgG molecules. SDS acrylamide gel analysis of injected rabbit IgG molecules revealed that heavy and light chains were degraded at the same rate. Injected rabbit IgGs and rabbit IgG fragments were also examined on isoelectric focusing gels. Fab, Fab2, and Fc fragments were degraded without any correlation with respect to isoelectric point. Positively charged rabbit IgGs disappeared more rapidly than their negative counterparts, contrary to the trend reported for normal intracellular proteins. The isoelectric points of two mouse monoclonal antibodies were essentially unchanged after injection into HeLa cells, ...Continue Reading

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Citations

Jan 10, 2013·Clinical Pharmacokinetics·Miroslav DostalekManoranjenni Chetty
Jan 1, 1984·Proceedings of the National Academy of Sciences of the United States of America·R Hough, M Rechsteiner
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May 6, 2008·Cancer Biotherapy & Radiopharmaceuticals·Tian YuanDai Guangfu
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