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Citation
Tags
HERO ID
1236307
Reference Type
Journal Article
Title
beta2-Microglobulins: isolation, properties, and distribution
Author(s)
Berggard, I
Year
1976
Is Peer Reviewed?
Yes
Journal
Federation Proceedings
ISSN:
0014-9446
Volume
35
Issue
5
Page Numbers
1167-1170
Language
English
PMID
57069
Abstract
beta2-Microglobulin is structurally related to immunoglobulin domains and is identical to the light chain of histocompatibility (HL-A) antigens. Similar to free light chains of immunoglobulins, beta2-microglobulin is most easily isolated from urine. We have previously purified human beta2-microglobulin from urine of patients with renal tubular resorption defects. Corresponding proteins have now been obtained from urine of rabbits and guinea pigs treated with sodium chromate. Sequence studies have established that the rabbit protein is rabbit beta2-microglobulin. The guinea pig protein closely resembles the human and rabbit beta2-microglobulins in amino acid composition, charge, molecular size, and also in the presence of an apparently analogous disulfide loop. These findings indicate that this protein is the guinea pig homologue of beta2-microglobulin. Physical-chemical studies suggest that human beta2-microglobulin and isolated immunoglobulin domains are similar not only in amino acid sequence but also in three-dimensional structure. Both types of molecules are compact and globular in shape and apparently contain beta-pleated sheet conformation. beta2-Microglobulin is present in free form in various body fluids and as a subunit of histocompatibility antigens on cell surfaces. Current estimates suggest that the number of beta2-microglobulin molecules on cell surfaces is higher than the number of histocompatibility (HL-A) antigens. Accordingly, beta2-microglobulin is possibly a subunit of additional cellular antigens or receptors.
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IRIS
•
Chromium VI
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Potentially Relevant Supplemental Material
Non-Peer Reviewed
Excluded
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