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hexapeptide/potato

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7 results

Analysis of epitopes on potato leafroll virus capsid protein.

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Pepscan hexapeptides prepared to the capsid protein amino acid sequence of potato leafroll luteovirus (PLRV) were tested against both polyclonal and monoclonal antibodies. Twelve continuous epitopes were identified: 11 were detected by two different PLRV polyclonal antisera, but only 4 were detected

Characterization of antigenic epitopes of potato virus Y.

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Immunochemical analysis of overlapping synthetic hexapeptides covering the entire length of the coat protein of potato virus Y (PVY) revealed immunodominant regions both at the N-terminal and at the C-terminal end of the coat protein. Immunization of rabbits with synthetic peptides representing N-

Peptidomics of Peptic Digest of Selected Potato Tuber Proteins: Post-Translational Modifications and Limited Cleavage Specificity.

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Bioinformatic tools are useful in predicting bioactive peptides from food proteins. This study was focused on using bioinformatics and peptidomics to evaluate the specificity of peptide release and post-translational modifications (PTMs) in a peptic digest of potato protein isolate. Peptides in the

Hydrolysis of the synthetic chromophoric hexapeptide Leu-Ser-Phe(NO2)-Nle-Ala-Leu-OMe catalyzed by bovine pepsin A. Dependence on pH and effect of enzyme phosphorylation level.

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Steady-state kinetic parameters for the hydrolysis of the chromophoric hexapeptide Leu-Ser-Phe(NO2)-Nle-Ala-Leu-OMe catalyzed by bovine gastricsin and pepsin A were determined. It was shown that the phosphate content of bovine pepsin A is without any significant effect on that parameters. At pH 4.7,

Dephosphorylation of synthetic phosphopeptides by protein phosphatase-T, a phosphothreonyl protein phosphatase.

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The synthetic phosphohexapeptides Arg-Arg-Ala-Thr(35P)-Val-Ala and Arg-Arg-Ala-Ser(32P)-Val-Ala, phosphorylated by the cAMP-dependent protein kinase and differing only in the nature of the phosphorylated residue, have been used as substrates of a partially purified rat liver protein phosphatase-T,

[Effect of the degree of phosphorylation of bovine pepsin A on its enzymatic activity].

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Proteolytic and clotting activities of bovine pepsin A with respect to its degree of phosphorylation were studied on various substrates. The occurrence of phosphate group(s) on bovine pepsin A more or less strongly affects its enzymic properties according to the substrate and its environment. This

Structure of ferric pseudobactin, a siderophore from a plant growth promoting Pseudomonas.

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Both plant growth promoting Pseudomonas B10 and its yellow-green, fluorescent iron transfer agent (siderophore) pseudobactin enhance the growth of the potato and control certain phytopathogenic microorganisms. The structure of the little compound has been determined by single-crystal X-ray
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