Scission réversible des isoagglutinines 19 S:
Etude de fixation des subunités

Jacot-Guillarmod, H.; Isliker, H

doi:10.1159/000464943

Cited by 7 publications

(2 citation statements)

References 3 publications

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“…However, neither the light ~,2-NTAbs nor the heavy 3,~-NTAbs lost their ability to fix to the kidneys after treatment with mercaptoethanol. This is in agreement with reports which have shown the persistence of the ability of subunits of/~2 macroglobulin to fix to antigens after mercaptoethanol treatment (23,24).…”

Section: Discussionsupporting

confidence: 93%

Experimental Glomerulonephritis

Unanue

Dixon

1965

The Journal of Experimental Medicine

123

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A direct correlation between the amount of kidney-fixing antibody and the degree of associated renal injury was demonstrated for rabbit and duck nephrotoxic antibodies. No evidence for a qualitative difference among nephrotoxic antibodies of a given type was obtained. It appeared that duck nephrotoxic antibody was directed against a wider spectrum of rat renal antigens than was rabbit nephrotoxic antibody. In order to produce immediate proteinuria an amount of rabbit or duck gamma-2 kidney-fixing antibody capable of occupying approximately 45 per cent or more of the capillary filtration surface was needed. For immediate proteinuria an amount of rabbit gamma-2 kidney-fixing antibody capable of reacting with more than one-half of the available antigenic sites was needed. Less than twice that amount of rabbit antibody completely saturated available antigenic sites in the kidney. Virtually all nephrotoxic antibodies in hyperimmune rabbit nephrotoxic sera were of the gamma-2 variety while nephrotoxic antibodies in comparable duck nephrotoxic sera were found in gamma-2 (with 5.8 and 7.4S sedimentation coefficients) and gamma-1M fractions. Gamma-1M duck nephrotoxic antibody was 60 times more potent a nephritogen than gamma-2 duck nephrotoxic antibody on a molecular basis. Mercaptoethanol abolished the nephrotoxicity of gamma-1M duck antibody and reduced that of gamma-2 duck antibodies but had no effect on rabbit gamma-2. In no case did mercaptoethanol treatment have an effect on the kidney-fixing properties of the antibodies involved. After injection of nephrotoxic antibodies there appeared to be a prompt fixation of a majority of the antibody to tissue antigens primarily in the kidney. However, a small amount of potentially kidney-fixing antibody remained in the circulation for a considerable period apparently reflecting a dissociation of less avid antibodies with an equilibrium between fixed and free antibody. The role of this more easily dissociable antibody in the progression of nephrotoxic nephritis is not certain but it is possible that it could play a role in the early progression of the disease.

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Section: Discussionsupporting

confidence: 93%

Experimental Glomerulonephritis

Unanue

Dixon

1965

The Journal of Experimental Medicine

123

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“…2) The 7 S IgM may possess univalent antibody activity as suggested by the finding of only indirect isohemagglutination, although further studies are necessary to establish this point with certainty. It is of interest that univalent-like antibody activity has been reported with the 7 S reductive subunits by several workers (15)(16)(17).…”

Section: Discussionmentioning

confidence: 99%

A Low Molecular Weight Immunoglobulin Antigenically Related to 19 S IgM*

Stobo¹,

Tomasi²

1967

J. Clin. Invest.

139

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Properties and modifications of a cryomacroglobulin possessing cold agglutinin activity

Deutsch

1969

Biopolymers

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synopsisThe physical properties of a pathological +-globulin with cold agglutinin activity and cryoglobulin solubility could be modified by changes in temperature and pH and upon dilution. The type of changes noted appear to simulate those expected in a readily dissociable antigen-antibody complex. Naturally occurring and chemically produced subunits of the +globulin and Fc-fragments of myeloma proteins diminished the cryoproperty of the +-globulin and effected changes in its physical properties but did not alter its cold agglutinin activity. Cryoglobulin properties could be conferred upon some purified +globulins by reacting them with Fc-fragments. Mercaptan dissociation of the cryomacroglobulin produces subunits with loss of the noted activities. Reaggregation of these subunits restores some of the native properties, but variable results which are dependent on the type of mercaptan employed are obtained. Attempts to explain the cold agglutinin activity of +globulin hybrids containing variable amounts of mercaptan-produced active and inert subunits suggest that activity requires two of the five subunits to be derived from the rM-cold agglutinin and to be adjacent to each other.

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Scission réversible des isoagglutinines 19 S: Etude de fixation des subunités

Cited by 7 publications

References 3 publications

Experimental Glomerulonephritis

Experimental Glomerulonephritis

A Low Molecular Weight Immunoglobulin Antigenically Related to 19 S IgM*

Properties and modifications of a cryomacroglobulin possessing cold agglutinin activity

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