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Of pea lectins

The software required for the quantitative evaluation and wavelength normalisation of Laue data has been successfully developed at Daresbury since the feasibility of recording full white beam Laue patterns from protein crystals was established. The software and the method have been tested using Laue data from crystals of pea lectin. As an example of the statistical quality (to 3 A resolution) the mean fractional change on F between monochromatic and Laue pea lectin data was 11 % and the same quantity between conventional source monochromatic and SR monochromatic pea lectin data is 8% (Helliwell et al., 1986). [Pg.50]

A thorough study of pea-lectin, carbohydrate-binding specificity was conducted by Van Wauwe and coworkers211 (see Table V). By hapten-... [Pg.199]

These experiments confirmed reduced exposure times and reductions in the relative amount of radiation damage over that on a conventional source (Fourme 1978, 1979 Kahn et al 1982a). In the Soviet Union on the VEPP-3 ring some preliminary data were collected by Mokulskaya (1981) using an electronic area detector in an attempt to optimise the anomalous dispersion of a platinum derivative of pea lectin crystals. [Pg.385]

D. Page, D. Zanini, and R. Roy, Macromolecular recognition Effect of multivalency in the inhibition of binding of yeast mannan to concanavalin A and pea lectins by mannosylated dendrimers, Bioorg. Med. Chem., 4 (1996) 1949-1961. [Pg.161]

Christensen et al. [93] successfully obtained a divalent cluster having -600-1500 enhanced binding properties. We have also demonstrated that dendritic mannosides such as 66 (Scheme 11) can provide up to 100-fold higher affinity (on a per-mannoside basis) when used to inhibit the binding of plant lectins (Concanavalin A and pea lectins) to yeast mannan [85]. As these interactions are at the origin of host infections by fimbriated bacteria, mannoside dendrimers can form the basis of novel antiadhesin molecules. [Pg.263]

Kornfeld, K., Reitman, M.-L. and Kornfeld, R. (1981). The carbohydrate-binding specificity of pea and lentil lectins. Fucose is an important determinant. Journal of Biological Chemistry, 256,6633-6640. [Pg.196]

Tryptic peptide mapping of each lectin revealed half of the expected number of peptides (15-16 peptides of the expected 32-37). The lectins share 15 identical, or closely similar, tryptic peptides441 this suggests that each protein is a molecule consisting of identical halves.441 However, a unique peptide was identified for LcH-A which stained gray with ninhydrin. The amino terminal sequence of the first 25 amino acids of the a- and /1-subunits of the pea and the lentil lectins has been determined. It was found that, of the 25 residues analyzed,442a,b,c the N-terminal cc-chain of the lentil and pea lectins differed only at three positions, and the /1-chains at two positions. [Pg.191]

Van Wauwe and coworkers182 studied the effect of various para-substituents on the binding of phenyl a-D-mannopyranosides to the lentil lectin. As with con A and the pea lectin, binding of p-substituted-phenyl a-D-mannopyranosides correlated fairly well with the Hammett substituent constant trH in which electron-releasing... [Pg.195]

In summary, the lentil lectins exhibit a carbohydrate-binding specificity similar to those of the pea lectin and con A primary specificity is towards a-D-mannopyranosyl residues (2), and secondary is to a-D-... [Pg.196]

The pea lectin binds a-D-Iinked D-glucobioses, but not /3-D-linked disaccharides (except for gentiobiose, which has one-eleventh the inhibitory effect of isomaltose). Like con A, it interacts with 2-0-(2-acetamido-2-deoxy-/3-D-gIucopyranosyI)-D-mannose, suggesting that it may be capable of binding to glycoproteins containing internal 2-0-substituted a-D-mannopyranosyl residues.210... [Pg.200]

Significant differences were found for the binding of methyl a- and j8-D-xylopyranoside to the pea lectin.211 These glycosides, lacking hydroxymethyl groups on C-5, are less effective, by factors of Va4oand s/ao,... [Pg.200]


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See also in sourсe #XX -- [ Pg.35 , Pg.197 ]




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