PMID: 3756184Oct 17, 1986Paper

Preparation and characterization of monoclonal antibodies to the extracellular hemoglobin of Lumbricus terrestris

Biochimica Et Biophysica Acta
J J LightbodyT Gotoh

Abstract

Murine monoclonal antibodies to the extracellular hemoglobin of Lumbricus terrestris were prepared by a modification of the method of Kohler and Milstein. 224 hybridomas were found to produce antibodies which bound to the hemoglobin; they were tested for binding to the four subunits of the hemoglobin: M (chain I, 16 kDa), D1 (chain V, 31 kDa), D2 (chain VI, 37 kDa) and T (50 kDa), a disulfide-bonded trimer of chains II, III and IV, each of about 17 kDa. 150 hybridomas bound to all four subunits and 40 hybridomas bound to various combinations of subunits. The remaining 34 hybridomas combined only with the hemoglobin. The twelve hybridomas obtained after subculturing and cloning were tested for their binding to the two fractions II and III, consisting of subunits D1 + D2 + T and M, respectively, obtained by dissociation at pH 9.5 and at pH 4.0 and to the reassociated whole molecules, obtained subsequent to return to neutral pH. Eight hybridomas which combined only with the hemoglobin also combined with all the reassociated molecules but not with any of the fractions: these monoclonal antibodies probably recognize conformation-dependent antigenic sites that are present only in the hexagonal bilayer structure characteristic of the ...Continue Reading

References

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Citations

Jan 1, 1988·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·J J LightbodyT Gotoh
Jan 1, 1985·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·S N Vinogradov
Mar 24, 2004·Micron : the International Research and Review Journal for Microscopy·Fumio Shishikura

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