JBC, Vol. 251, Issue 19, 5929-5935, Oct, 1976
Purification and characterization of two lectins from Caragana arborescens seeds
R. Bloch, J. Jenkins, J. Roth and M. M. Burger
A glycoprotein fraction with hemagglutinating activity was purified by
affinity chromatography from seeds of the pea tree, Caragana arborescens.
Subsequent fractionation resolved two components, which could be separated
on a preparative scale using different affinity matrices. The major
component binds to N-acetylgalactosamine coupled to Sepharose 4B. It is a
glycoprotein with high hemagglutinating activity. It is composed of two
types of polypeptides, present in nonstoichiometric amounts, with apparent
molecular weights near 30,000. In the native molecule, the subunits are
cross-linked by disulfide bonds to form dimers, which in turn appear to be
in rapid equilibrium with tetramers. The minor component binds to
underivatized Sepharose 4B. It too, is a glycoprotein but has low
hemagglutinating activity. It is composed of three types of polypeptides
which, although they have apparent molecular weights near 30,000 are
distinguished from the subunits of the major hemagglutinin by a number of
physical and chemical properties. The native molecule is dimeric, with a
mass of 60,000 daltons. The major component has high affinity (K = 0.1 mM)
for the haptenic sugar, N-acetylgalactosamine, but will also bind
D-galactose. Neither lectin has ABO blood group specificity, nor are they
transformed mouse fibroblasts to the same extent.
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