TY - JOUR
T1 - Precipitation of Concanavalin A by a high mannose type glycopeptide
AU - Bhattacharyya, Lokesh
AU - Brewer, C. Fred
N1 - Funding Information:
The authors wish to thank Drs. Jorgen Lonngren, Pharmacia Fine Chemicals, Uppsala, Sweden, and William Chaney, Albert Einstein College of Medicine, Bronx, New York for generous gifts of carbohydrates. This work was supported by Grant CA-16054 from the National Cancer Institute, Department of Health, Education, and Welfare, and Core Grant P30 CA-13330 from the same agency.
PY - 1986/6/13
Y1 - 1986/6/13
N2 - The interactions of a high mannose type glycopeptide with Concanavalin A has been investigated by quantitative precipitation analysis. The equivalence points of the precipitin curves indicate that the glycopeptide is bivalent for lectin binding. These results and others demonstrate that there are two lectin binding sites per molecule of the glycopeptide: one site on the α(1-6) arm of the core β-mannose residue involving a trimannosyl moiety, and another site on the α(1-3) arm of the core β-mannose residue involving an α(1-2) mannobiosyl group. The two sites are unequal in their affinities, and bind by different mechanisms. These results are related to the possible structure-function properties of high mannose type of glycopeptides on the surface of cells.
AB - The interactions of a high mannose type glycopeptide with Concanavalin A has been investigated by quantitative precipitation analysis. The equivalence points of the precipitin curves indicate that the glycopeptide is bivalent for lectin binding. These results and others demonstrate that there are two lectin binding sites per molecule of the glycopeptide: one site on the α(1-6) arm of the core β-mannose residue involving a trimannosyl moiety, and another site on the α(1-3) arm of the core β-mannose residue involving an α(1-2) mannobiosyl group. The two sites are unequal in their affinities, and bind by different mechanisms. These results are related to the possible structure-function properties of high mannose type of glycopeptides on the surface of cells.
UR - http://www.scopus.com/inward/record.url?scp=0022470920&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0022470920&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(86)91130-7
DO - 10.1016/0006-291X(86)91130-7
M3 - Article
C2 - 3729933
AN - SCOPUS:0022470920
SN - 0006-291X
VL - 137
SP - 670
EP - 674
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -