Application of heptapeptides containing D-amino acid residues immobilized to magnetic particles and Sepharose for the study of binding properties of gastric aspartic proteases |
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Authors: | Rajčanová Michaela Tichá Marie Kučerová Zdenka |
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Institution: | Institute of Pathophysiology, First Faculty of Medicine, Charles University in Prague, Prague, Czech Republic. |
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Abstract: | Synthetic heptapeptides containing D-amino acid residues and differing in the content of L-phenylalanine and L-tyrosine residues and their position (Val-D-Leu-Pro-Tyr-Phe-Val-D-Leu, Val-D-Leu-Pro-Tyr-Tyr-Val-D-Leu, Val-D-Leu-Pro-Phe-Tyr-Val-D-Leu) were immobilized to two types of carriers: glyoxal-activated magnetic agarose particles and CNBr-activated Sepharose. In both cases, peptides were immobilized via their terminal amino group. Immobilized peptides were used for the study of binding properties of two gastric aspartic proteases (porcine pepsin A and rat pepsin C). Porcine pepsin A was adsorbed to all studied peptide-modified magnetic carriers, while rat pepsin C interacted with immobilized ligands only slightly. Similar results were obtained in affinity chromatographic experiments using heptapeptides immobilized to Sepharose. |
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Keywords: | Immobilized heptapeptides Magnetic particles Porcine pepsin A Rat pepsin C Sepharose |
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