Dimer formation of a cell-cell adhesion protein, gp64 of the cellular slime mold, Polysphondylium pallidum [Myxomycetes]
1996
Ochiai, H. (Hokkaido Univ., Sapporo (Japan)) | Hata, K. | Saito, T. | Funamoto, S. | Nakata, N.
The cellular slime mold, Polysphondylium pallidum, has two EDTA-resistant types of cell-cell adhesion. The major component of them has been identified as a glycoprotein with a molecular mass of 64 kDa on SDS-PAGE (referred to as gp64). We found that a substantial amount of the gp64 run as dimer, when gp64 was dissolved in SDS-sample buffer without 2-mercaptoethanol and then subjected to electrophoresis. The occurrence of a homophilic dimer was demonstrated by analyzing the dimer-like band on a gel for its amino acid sequence and amino acid composition. The dimer-like band also was analyzed by three sorts of monoclonal antibodies, two of which recognize respectively a conformational epitope and a denatured epitope of the protein moiety of gp64. The data indicate that the native conformation of gp64 is necessary for dimer formation
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