A REACTION BETWEEN SOME STREPTOCOCCI AND IgA MYELOMA PROTEINS

Myeloma-like immune globulins present themselves as narrow bands upon paper electrophoresis, and usually show a characteristic appearance in immunoelectrophoresis. Two antigenically different groups of myeloma proteins have been described: groups I and II. Recently, 60% of normal γ-globulin, throughout the mobility range of γ-globulin, has been shown to possess the antigen characteristic for group I, and 30% that for group II myeloma. Occurrence of myeloma-like proteins in the serum is not restricted to multiple myeloma. They may also be seen with other tumors, such as reticulum cell sarcoma, and various carcinomas. In addition, Sonnet and Milhaux have reported on the frequent occurrence of myeloma-like ("monoclonal") γ-globulins in the serum of adult Bantus with different diseases. When large amounts of a myeloma protein are present in the serum, it may be found in a much lower concentration in the spinal fluid.

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Structural Differences in the Hinge Region of Human Gamma A Myeloma Proteins of Different Subclasses

Nature New Biology ◽

10.1038/newbio233029a0 ◽

1971 ◽

Vol 233 (35) ◽

pp. 29-31 ◽

Cited By ~ 15

Author(s):

CARLOS A. ABEL ◽

HOWARD M. GREY

Keyword(s):

Hinge Region ◽

Myeloma Proteins ◽

Structural Differences

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Myeloma Proteins (M-Components) with Antibody-like Activity

New England Journal of Medicine ◽

10.1056/nejm197104152841507 ◽

1971 ◽

Vol 284 (15) ◽

pp. 831-838 ◽

Cited By ~ 60

Author(s):

Michael Potter

Keyword(s):

Myeloma Proteins

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IMMUNOLOGICAL STUDIES OF HUMAN γ-GLOBULIN

Journal of Experimental Medicine ◽

10.1084/jem.112.1.203 ◽

1960 ◽

Vol 112 (1) ◽

pp. 203-223 ◽

Cited By ~ 120

Author(s):

G. M. Edelman ◽

J. F. Heremans ◽

M.-Th. Heremans ◽

H. G. Kunkel

Keyword(s):

Deae Cellulose ◽

Antigenic Determinants ◽

Agar Diffusion ◽

Myeloma Proteins ◽

Zone Electrophoresis ◽

Γ Globulins

Two major antigenic fragments were obtained from various purified γ-globulin preparations after papain treatment. One, the F component, had a mobility faster than the original γ-globulin and the second, the S component, had a slower mobility. Similar F and S components were also obtained with certain homogeneous myeloma proteins which were closely related to γ-globulin immunologically. Additional minor antigenic components were detected with certain antisera. The technique of immunoelectrophoresis was particularly useful for bringing out the different antigenic constituents obtained after papain treatment. The F and S components as well as a midfraction were isolated by chromatography on DEAE-cellulose. These were immunologically homogeneous and could be utilized to absorb F and S antibodies from various antisera. The relative amount of F and S antibodies varied in different antisera from individual rabbits immunized with whole γ-globulin. Whole γ-globulin was separated by zone electrophoresis into a fast migrating and a more slowly migrating fraction. Each of these gave rise to F and S components after splitting with papain. The F components of the two γ-globulins were similar in mobility, while the S components showed marked mobility differences although antigenically they were very similar. The mobility differences of the parent γ-globulin appeared to be primarily related to the differences in the S component. Certain antisera against pathological γ-globulins were found to give double lines with a wide variety of γ-globulin preparations in agar diffusion. These were shown to be related to the F and S antigenic determinants of γ-glubulin. This relationship was evident by a number of procedures utilizing both Ouchterlony plate techniques and immunoelectrophoresis. The question of whether these findings indicate heterogeneity of γ-globulin in relation to the F and S antigenic components, or whether different antigenic groups on one molecule can give rise to separate lines in certain instances, is discussed.

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