TY - JOUR
T1 - Comparison of the spectroscopic and saccharide binding properties of lentil and pea isolectins
AU - Bhattacharyya, Lokesh
AU - Freedman, Jonathan H.
AU - Brewer, C. Fred
AU - Brown, Rodney D.
AU - Koenig, Seymour H.
N1 - Funding Information:
The authors thank Mr. Bert Olson of IBM Thomas J. Watson Research Center for the atomic absorption analysis. This work was supported in part by Grant CA 16054, awarded to C.F.B. by the National Cancer Institute, Department of Health, Education and Welfare, and NIH/NCI Core Grant P30 CA 13330.
PY - 1985/8/1
Y1 - 1985/8/1
N2 - The lentil isolectins, CMLcH A and CMLcH B, and pea isolectins, CMPSA A and CMPSA B, are compared in terms of their spectroscopic and saccharide binding properties. The paramagnetic contribution to the solvent proton magnetic relaxation dispersion profiles of solutions of the isolectins of each protein are found to be essentially identical. Electron paramagnetic resonance spectra suggest a high degree of octahedral symmetry at the Mn2+ site for both pairs of isolectins. The near-ultraviolet absorption spectra of CMLcH A and CMLcH B are identical, as are the spectra of CMPSA A and CMPSA B. Carbohydrate binding activities of the isolectins of each protein are compared using hemagglutination, precipitation, and precipitation-inhibition assays, and are found to be identical, although the activities of CMLcH and CMPSA differ somewhat. These results demonstrate that the spectroscopic and saccharide binding properties of the isolectins of CMLcH are essentially identical, as are those of the isolectins of CMPSA, and suggest that native mixtures of the isolectins may be treated as single proteins in further studies.
AB - The lentil isolectins, CMLcH A and CMLcH B, and pea isolectins, CMPSA A and CMPSA B, are compared in terms of their spectroscopic and saccharide binding properties. The paramagnetic contribution to the solvent proton magnetic relaxation dispersion profiles of solutions of the isolectins of each protein are found to be essentially identical. Electron paramagnetic resonance spectra suggest a high degree of octahedral symmetry at the Mn2+ site for both pairs of isolectins. The near-ultraviolet absorption spectra of CMLcH A and CMLcH B are identical, as are the spectra of CMPSA A and CMPSA B. Carbohydrate binding activities of the isolectins of each protein are compared using hemagglutination, precipitation, and precipitation-inhibition assays, and are found to be identical, although the activities of CMLcH and CMPSA differ somewhat. These results demonstrate that the spectroscopic and saccharide binding properties of the isolectins of CMLcH are essentially identical, as are those of the isolectins of CMPSA, and suggest that native mixtures of the isolectins may be treated as single proteins in further studies.
UR - http://www.scopus.com/inward/record.url?scp=0022260878&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0022260878&partnerID=8YFLogxK
U2 - 10.1016/0003-9861(85)90091-8
DO - 10.1016/0003-9861(85)90091-8
M3 - Article
C2 - 2992383
AN - SCOPUS:0022260878
SN - 0003-9861
VL - 240
SP - 820
EP - 826
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 2
ER -