Abstract
Aminopropyl Perloza beaded cellulose was used as the support for solid-phase synthesis of resin-bound Val-dLeu-Pro-Phe-Phe-Val-dLeu, an inhibitor of aspartic proteases. Both Boc and Fmoc SPPS methodologies were employed in separate syntheses. The peptide-resins were characterized by amino acid analysis. The peptide-resin from the Fmoc synthesis gave the better amino acid analysis of the two syntheses and was used for further studies. Following modification of the peptide N-terminus by succinylation, the peptide-resin was able to bind chymosin (E.C. 3.5.21.4). The peptide resin was used for isolation of chymosin from a crude recombinant broth.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amino Acids
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Aspartic Acid Endopeptidases / antagonists & inhibitors
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Cellulose
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Chromatography, Affinity*
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Chymosin / isolation & purification*
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Chymosin / metabolism
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Fluorenes
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Formic Acid Esters
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Ligands
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Molecular Sequence Data
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Oligopeptides / chemical synthesis*
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Oligopeptides / metabolism
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Protease Inhibitors / chemical synthesis*
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Protease Inhibitors / chemistry
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Recombinant Proteins / isolation & purification
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Resins, Plant
Substances
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Amino Acids
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Fluorenes
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Formic Acid Esters
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Ligands
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N(alpha)-fluorenylmethyloxycarbonylamino acids
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Oligopeptides
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Protease Inhibitors
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Recombinant Proteins
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Resins, Plant
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t-butyloxycarbonyl group
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succinyl-valyl-leucyl-prolyl-phenylalanyl-phenylalanyl-valyl-leucinamide
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Cellulose
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Aspartic Acid Endopeptidases
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Chymosin