Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 353-359 |
| Number of pages | 7 |
| Journal | Journal of Protein Chemistry |
| Volume | 19 |
| Issue number | 5 |
| DOIs | |
| State | Published - Dec 1 2000 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
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The isolation and properties of the dimeric subunit of Concanavalin A. / Pazur, John H.; Perloff, Michael D.; Frymoyer, Adam R.; Jensen, Carolyn J.P.; Micolochick, Holly; Mastro, Andrea Marie.
In: Journal of Protein Chemistry, Vol. 19, No. 5, 01.12.2000, p. 353-359.Research output: Contribution to journal › Article
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 Marie
PY - 2000/12/1
Y1 - 2000/12/1
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.
UR - http://www.scopus.com/inward/record.url?scp=0034529021&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034529021&partnerID=8YFLogxK
U2 - 10.1023/A:1026431329188
DO - 10.1023/A:1026431329188
M3 - Article
C2 - 11131142
VL - 19
SP - 353
EP - 359
JO - Protein Journal
JF - Protein Journal
SN - 1572-3887
IS - 5
ER -