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KMID : 0578319930030020221
Molecules and Cells
1993 Volume.3 No. 2 p.221 ~ p.224
Characaterization of Agglutinating Monoclonal Antibody against Human Red Blood Cells
Nham, Sang-Uk
Im, Suhn-young/Lee, Kee-Soon/Cho, Seo-Hee/Lee, Young Ik
Abstract
As a first step to clone cDNAs encoding variable domains of the heavy and the fight chain of hemagglutinating antibody, mouse monoclonal antibodies against human red blood cells were generated and the N-termini of the heavy and the fight chain were sequenced. Ficollpaque purified red blood cells were used as a antigen to generate hybridoma and nine clones were selected as positive clones by a hemagglutination assay. One clone (# 12) was selected as a strong antibody producer and monoclonal antibody secreted from the clone was purified to homogeneity. By amino acid analysis, N-terminal sequence of the heavy chain was shown to be Glu-Val-Gin-L eu-Gin-Gin-Ser-Gly-Pro and that of the fight chain was Asp-Ile-Val-Met-Thr-Gln-Ser-Pro. The heavy chain sequence was identified as antibody subgroup Ha and that of the light chain was subgroup I or subgroup III. Taken together, these results provided useful information to design ofigonucleotides for cloning of antibody cDNA which is initial phase work toward developing immunodiagnostic using human whole blood.
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