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 | Zendy

Rajčanová Michaela | Zendy; Tichá Marie | Zendy; Kučerová Zdenka | Zendy

Premium

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research