TY - JOUR
T1 - The isolation and properties of the dimeric subunit of Concanavalin A
AU - Pazur, John H.
AU - Perloff, Michael D.
AU - Frymoyer, Adam R.
AU - Jensen, Carolyn J.P.
AU - Micolochick, Holly
AU - Mastro, Andrea
PY - 2000
Y1 - 2000
N2 - Concanavalin A (Con A) was dissociated into dimeric and monomeric subunits by incubation at 37°C in acetate buffer of pH 3.8 containing 0.5% sodium dodecyl sulfate. The dimer was isolated in pure form by a density gradient ultracentrifugation method. Several properties of the dimer were determined including the formation of a precipitin with anti-Con A antibodies, the molecular weight, the lack of a binding site for glycogen, the lack of mitogenic activity for spleen lymphocytes, and the lack of inhibition by α-methyl D-glucoside. The latter findings differ from results reported by other investigators.
AB - Concanavalin A (Con A) was dissociated into dimeric and monomeric subunits by incubation at 37°C in acetate buffer of pH 3.8 containing 0.5% sodium dodecyl sulfate. The dimer was isolated in pure form by a density gradient ultracentrifugation method. Several properties of the dimer were determined including the formation of a precipitin with anti-Con A antibodies, the molecular weight, the lack of a binding site for glycogen, the lack of mitogenic activity for spleen lymphocytes, and the lack of inhibition by α-methyl D-glucoside. The latter findings differ from results reported by other investigators.
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U2 - 10.1023/A:1026431329188
DO - 10.1023/A:1026431329188
M3 - Article
C2 - 11131142
AN - SCOPUS:52849098107
SN - 0277-8033
VL - 19
SP - 353
EP - 359
JO - Journal of Protein Chemistry
JF - Journal of Protein Chemistry
IS - 5
ER -