Characterization of immunoglobulin A kappa autoantibodies to human lactate dehydrogenase isoenzyme-3

R. N. Weijers; R. P. Oude Elferink; J. Mulder; H. Kruijswijk

doi:https://doi.org/10.1016/0090-1229(87)90178-4

Characterization of immunoglobulin A kappa autoantibodies to human lactate dehydrogenase isoenzyme-3

R. N. Weijers, R. P. Oude Elferink, J. Mulder, H. Kruijswijk

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Abstract

We have purified with a cumulative recovery of 48% from the serum of a patient the immunoglobulin A kappa subunit of the lactate dehydrogenase-immunoglobulin A kappa (LD-IgA kappa) complex. It appears that the pI range of the complex is 5.4-5.8. The Ig part of the complex showed a monoclonal character, and the complex exhibited a 1:2 molar ratio of the Ig to the LD isoenzyme. From reconstitution experiments by two different methods we concluded that LD-3 is essential for restoring the original complex. Additional studies showed a recombination of the IgA kappa with both autologous and homologous LD-3, and a binding of LD-3 at the Fab region of the Ig. The estimated value of the affinity constant (Keq) was 2.1 X 10(9) liters/mol. Analysis of the specific LD-3-binding IgA kappa concentrations in the sera of five cases revealed a broad range of the individual immune response. Our first quantitative data on the lymphocyte subpopulations revealed a significantly increased OKT4/OKT8 ratio due to a reduction in the absolute number of T suppressor cells

Original language	English
Pages (from-to)	110-122
Journal	Clinical immunology and immunopathology
Volume	42
Issue number	1
DOIs	https://doi.org/10.1016/0090-1229(87)90178-4
Publication status	Published - 1987

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https://doi.org/10.1016/0090-1229(87)90178-4

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@article{6dcb86a2a238429c83f6f15244fe158f,

title = "Characterization of immunoglobulin A kappa autoantibodies to human lactate dehydrogenase isoenzyme-3",

abstract = "We have purified with a cumulative recovery of 48% from the serum of a patient the immunoglobulin A kappa subunit of the lactate dehydrogenase-immunoglobulin A kappa (LD-IgA kappa) complex. It appears that the pI range of the complex is 5.4-5.8. The Ig part of the complex showed a monoclonal character, and the complex exhibited a 1:2 molar ratio of the Ig to the LD isoenzyme. From reconstitution experiments by two different methods we concluded that LD-3 is essential for restoring the original complex. Additional studies showed a recombination of the IgA kappa with both autologous and homologous LD-3, and a binding of LD-3 at the Fab region of the Ig. The estimated value of the affinity constant (Keq) was 2.1 X 10(9) liters/mol. Analysis of the specific LD-3-binding IgA kappa concentrations in the sera of five cases revealed a broad range of the individual immune response. Our first quantitative data on the lymphocyte subpopulations revealed a significantly increased OKT4/OKT8 ratio due to a reduction in the absolute number of T suppressor cells",

author = "Weijers, {R. N.} and {Oude Elferink}, {R. P.} and J. Mulder and H. Kruijswijk",

year = "1987",

doi = "https://doi.org/10.1016/0090-1229(87)90178-4",

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TY - JOUR

T1 - Characterization of immunoglobulin A kappa autoantibodies to human lactate dehydrogenase isoenzyme-3

AU - Weijers, R. N.

AU - Oude Elferink, R. P.

AU - Mulder, J.

AU - Kruijswijk, H.

PY - 1987

Y1 - 1987

N2 - We have purified with a cumulative recovery of 48% from the serum of a patient the immunoglobulin A kappa subunit of the lactate dehydrogenase-immunoglobulin A kappa (LD-IgA kappa) complex. It appears that the pI range of the complex is 5.4-5.8. The Ig part of the complex showed a monoclonal character, and the complex exhibited a 1:2 molar ratio of the Ig to the LD isoenzyme. From reconstitution experiments by two different methods we concluded that LD-3 is essential for restoring the original complex. Additional studies showed a recombination of the IgA kappa with both autologous and homologous LD-3, and a binding of LD-3 at the Fab region of the Ig. The estimated value of the affinity constant (Keq) was 2.1 X 10(9) liters/mol. Analysis of the specific LD-3-binding IgA kappa concentrations in the sera of five cases revealed a broad range of the individual immune response. Our first quantitative data on the lymphocyte subpopulations revealed a significantly increased OKT4/OKT8 ratio due to a reduction in the absolute number of T suppressor cells

AB - We have purified with a cumulative recovery of 48% from the serum of a patient the immunoglobulin A kappa subunit of the lactate dehydrogenase-immunoglobulin A kappa (LD-IgA kappa) complex. It appears that the pI range of the complex is 5.4-5.8. The Ig part of the complex showed a monoclonal character, and the complex exhibited a 1:2 molar ratio of the Ig to the LD isoenzyme. From reconstitution experiments by two different methods we concluded that LD-3 is essential for restoring the original complex. Additional studies showed a recombination of the IgA kappa with both autologous and homologous LD-3, and a binding of LD-3 at the Fab region of the Ig. The estimated value of the affinity constant (Keq) was 2.1 X 10(9) liters/mol. Analysis of the specific LD-3-binding IgA kappa concentrations in the sera of five cases revealed a broad range of the individual immune response. Our first quantitative data on the lymphocyte subpopulations revealed a significantly increased OKT4/OKT8 ratio due to a reduction in the absolute number of T suppressor cells

U2 - https://doi.org/10.1016/0090-1229(87)90178-4

DO - https://doi.org/10.1016/0090-1229(87)90178-4

M3 - Article

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SN - 0090-1229

VL - 42

SP - 110

EP - 122

JO - Clinical immunology and immunopathology

JF - Clinical immunology and immunopathology

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