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PMID: 4558655 Published · ppublish English Journal Article

2 -Microglobulin--a free immunoglobulin domain.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 69 ·No. 7 ·1972-07-00 ·Pages 1697-701

Peterson PA, Cunningham BA, Berggård I, Edelman GM

Abstract

Analysis of the primary structure of beta(2)-microglobulin indicates that this human protein is homologous in sequence to the constant portion of immunoglobulin light chains (C(L)), and to the homology regions (C(H)1, C(H)2, and C(H)3) of the constant portion of gamma1 (heavy) chains of immunoglobulin G. Homology with the C(H)3 region is particularly striking. No convincing homology could be demonstrated by similar comparisons with the variable regions of immunoglobulin light and heavy chains. beta(2)-Microglobulin contains an intrachain disulfide loop of 57 amino-acid residues that is similar in size to disulfide loops found in the constant regions of immunoglobulin G. These findings suggest that beta(2)-microglobulin is a free immunoglobulin domain, possibly serving an effector function similar to that of the C(H)3 domain of gamma1 chains of immunoglobulin G.

MeSH Terms
Amino Acid Sequence Animals Blood Proteins/analysis Cadmium Poisoning/urine Chymotrypsin Humans Immunoglobulin G Immunoglobulins Iodine Isotopes Leukocytes/analysis Pepsin A Poisoning/urine Protein Binding Proteinuria/chemically induced Rabbits/immunology Thermolysin Trypsin
Chemicals
Blood Proteins Immunoglobulin G Immunoglobulins Iodine Isotopes Chymotrypsin Trypsin Pepsin A Thermolysin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Peterson P A
Cunningham B A
Berggård I
Edelman G M
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23 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.69.7.1697
Published
1972-07-00
Pages
1697-701
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC426781
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.69.7.1697 PMC Full Text View journal details
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