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Application of heptapeptides containing D ‐amino acid residues immobilized to magnetic particles and S epharose for the study of binding properties of gastric aspartic proteases
Author(s) -
Rajčanová Michaela,
Tichá Marie,
Kučerová Zdenka
Publication year - 2012
Publication title -
journal of separation science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.72
H-Index - 102
eISSN - 1615-9314
pISSN - 1615-9306
DOI - 10.1002/jssc.201200221
Subject(s) - chemistry , chromatography , pepsin , peptide , amino acid , agarose , aspartic acid , proteases , phenylalanine , biochemistry , enzyme
Synthetic heptapeptides containing D ‐amino acid residues and differing in the content of L ‐phenylalanine and L ‐tyrosine residues and their position ( V al‐ D ‐ L eu‐ P ro‐ T yr‐ P he‐ V al‐ D ‐ L eu, V al‐ D ‐ L eu‐ P ro‐ T yr‐ T yr‐ V al‐ D ‐ L eu, V al‐ D ‐ L eu‐ P ro‐ P he‐ T yr‐ V al‐ D ‐ L eu) were immobilized to two types of carriers: glyoxal‐activated magnetic agarose particles and CNB r‐activated S epharose. 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 S epharose.