HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Miller, F. Articles by Metzger, H. Search for Related Content PubMed PubMed Citation Articles by Miller, F. Articles by Metzger, H. Social Bookmarking                      What's this?

Characterization of a Human Macroglobulin

III. THE PRODUCTS OF TRYPTIC DIGESTION

From the ¹ From the Arthritis and Rheumatism Branch, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland 20014

A human Waldenström macroglobulin (M) and its subunits (M_s) were subjected to tryptic hydrolysis. A fragment was isolated which was relatively stable to further tryptic attack. It had a molecular weight of 47,000, contained a single interchain disulfide bond, and both heavy (µ) chain and light () chain antigenic determinants. After reduction, the latter were separable by Sephadex chromatography in 1 n propionic acid. A second fragment with a molecular weight of 114,000 was isolated and appeared to be a dimer consisting of two fragments, somewhat larger than the above, linked by way of the µ chain pieces by a single disulfide bond. The similarity of these fragments to those obtainable by enzymatic digestion of 7 S ₂-globulin immunoglobulins was documented, and it is suggested that they be called Fabµ and F(ab')₂µ, respectively.

It is proposed on the basis of these studies that human macroglobulin molecules have potentially 10 antibody combining sites.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				C. Paul, A. Shimizu, H. Kohler, and F. W. Putnam Structure of the Hinge Region of the Mu Heavy Chain of Human IgM Immunoglobulins Science, April 2, 1971; 172(3978): 69 - 72. [Abstract] [PDF]

				K. Onoue, A. L. Grossberg, Y. Yagi, and D. Pressman Imnunoglobulin M Antibodies with Ten Combining Sites Science, November 1, 1968; 162(3853): 574 - 576. [Abstract] [PDF]

				S-E. Svehag, B. Chesebro, and B. Bloth Ultrastructure of Gamma M Immunoglobulin and Alpha Macroglobulin: Electron-Microscopic Study Science, November 17, 1967; 158(3803): 933 - 936. [Abstract] [PDF]

				R. F. Doolittle, S. J. Singer, and H. Metzger Evolution of Immunoglobulin Polypeptide Chains: Carboxy-Terminal of an IgM Heavy Chain Science, December 23, 1966; 154(3756): 1561 - 1562. [Abstract] [PDF]