TY - JOUR
T1 - Formation of homogeneous cross-linked lattices between oligomannose type glycopeptides and concanavalin A
AU - Islam Khan, M.
AU - Bhattacharyya, Lokesh
AU - Brewer, C. Fred
N1 - Funding Information:
We wish to thank Dr. William Chaney of the University of Nebraska Medical Center and Dr. Pamela Stanley of Albert Einstein College of Medicine for a generous gift of the Man-6 glycopeptide. 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. The NMR facility at Albert Einstein College of Medicine was supported by Instrumentation Grants I-SI0-RR02309 from the National Institute of Health and DMB-8413723 from the National Science Foundation.
PY - 1988/5/16
Y1 - 1988/5/16
N2 - Certain oligomannose type glycopeptides have previously been shown to be bivalent for binding to concanavalin A, and to give quantitative precipitation profiles with the protein that consist of single peaks which correspond to the binding stoichiometry of glycopeptide to protein monomer (1:2) (Bhattacharyya, L., Ceccarini, C., Lorenzoni, P., and Brewer, C.F. (1987) J. Biol. Chem. 262, 1288-1293). In the present study, equimolar mixtures of two oligomannose type glycopeptides, a Man-6 and a Man-9 glycopeptide, gives a quantitative precipitation profile which shows two protein peaks. Each glycopeptide was radiolabelled with 3H or 14C, and the the precipitation profiles of the individual glycopeptides in the mixture determined. The results show that the radioactivity profile of the Man-6 glycopeptide corresponds to the first protein peak, while the radioactivity profile of the Man-9 glycopeptide corresponds to the second protein peak. The results indicate that each glycopeptide forms a unique homogeneous cross-linked lattice with the lectin which excludes the lattice of the other glycopeptide.
AB - Certain oligomannose type glycopeptides have previously been shown to be bivalent for binding to concanavalin A, and to give quantitative precipitation profiles with the protein that consist of single peaks which correspond to the binding stoichiometry of glycopeptide to protein monomer (1:2) (Bhattacharyya, L., Ceccarini, C., Lorenzoni, P., and Brewer, C.F. (1987) J. Biol. Chem. 262, 1288-1293). In the present study, equimolar mixtures of two oligomannose type glycopeptides, a Man-6 and a Man-9 glycopeptide, gives a quantitative precipitation profile which shows two protein peaks. Each glycopeptide was radiolabelled with 3H or 14C, and the the precipitation profiles of the individual glycopeptides in the mixture determined. The results show that the radioactivity profile of the Man-6 glycopeptide corresponds to the first protein peak, while the radioactivity profile of the Man-9 glycopeptide corresponds to the second protein peak. The results indicate that each glycopeptide forms a unique homogeneous cross-linked lattice with the lectin which excludes the lattice of the other glycopeptide.
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U2 - 10.1016/S0006-291X(88)80394-2
DO - 10.1016/S0006-291X(88)80394-2
M3 - Article
C2 - 3377767
AN - SCOPUS:0023894997
SN - 0006-291X
VL - 152
SP - 1076
EP - 1082
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -