Pea lectin

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. 

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). 

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. 

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. 

Like the jack-bean and pea lectins, the lentil agglutinin interacted with 2-0-(2-acetamido-2-deoxy-j8-D-glucopyranosyI)-D-mannose,210 providing evidence that the lentil lectin binds to internal 2-0-substituted D-mannopyranosyl residues that occur in animal glycoproteins. 

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... 

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-... 

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

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... 

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,... 

The pea lectin precipitated with muscle glycogen, yeast mannan from Saccharomyces cerevisiae, and O-phosphonomannan from Pichia pinus.122 All of these reactions were inhibited by specific, sugar haptens (D-mannose, D-glucose, and D-fructose).122... 

The pea lectin, like con A, agglutinated normal, embryonic fibroblasts of human and rat origin at high lectin concentrations (1.500 mg/ ml), whereas, various, rat tumor-cells transformed in vitro (spontaneously, and by Rous sarcoma virus) were agglutinated at very low concentrations (5 pg/ml) of lectin.460... 

Pospisilova and coworkers185 investigated the chemical structure of the pea lectin-reactive glycopeptide isolated by Kubanek and coworkers.844 After refining the chemical analysis, and applying glycosidase digestion, they proposed the structure depicted in formula 16. Despite... 

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