Trifluoroacetic acid → L-Glutamic Acid

HRID 361779Notizen

Reaktionsgleichung

Reaktionsgleichung von HRID 361779
OC[C:3]([CH2:7]O)([CH2:5][OH:6])[NH2:4].[Cl-].[Cl-].[Ca+2].F[C:13](F)(F)[C:14]([OH:16])=[O:15].FC(F)(F)C(O)=[O:22].C(#N)C>>[NH2:4][C@H:3]([C:5]([OH:6])=[O:22])[CH2:7][CH2:13][C:14]([OH:16])=[O:15]

Komponenten

5

Versuchsvorschrift

The oligopeptides prepared as described in Example 2 were individually dissolved in PSA digestion buffer (12 mM tris(hydroxymethyl)-aminomethane pH8.0, 25 mM NaCl, 0.5 mM CaCl2) and the solution added to PSA at a molar ration of 100 to 1. The reaction is quenched after various reaction times by the addition of trifluoroacetic acid (TFA) to a final 1% (volume/volume). The quenched reaction was analyzed by HPLC on a reversed-phase C18 column using an aqueous 0.1% TFA/acetonitrile gradient.The results of the assessment are shown in FIG. 2. Other oligopeptides prepared as described in Example 2 were tested in the same assay wherein the reaction was quenched at 4 hours. Those results of the assessment are shown in FIG. 3. The removal of an asparagine residue from the amino terminus of the oligopeptide results in a significant loss of PSA mediatedpeptide hydrolysis, while the presence of a glutamic acid residue at the carboxyl end of the peptide appears not to be essential to recognition by PSA.

Aufarbeitung

  1. customThe reaction is quenched
  2. customafter various reaction times
  3. customThe quenched reaction
  4. customgradient.The results of the assessment
  5. customwas quenched at 4 hours
  6. customThose results of the assessment
  7. customThe removal of an asparagine residue from the amino terminus of the oligopeptide

Quellen und Nachweise

ORD-Eintrag
ord-8991477dc1df4caab9732905b6154c95
Quelldatensatz
uspto-grants-1999_02
Patentnummer
US05866679

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