6
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      First report on a potato I family chymotrypsin inhibitor from the seeds of a Cucurbitaceous plant, Momordica cochinchinensis.

      Biological chemistry

      Amino Acid Sequence, Chromatography, Affinity, Chromatography, High Pressure Liquid, methods, Chymotrypsin, antagonists & inhibitors, Molecular Sequence Data, Molecular Weight, Momordica, enzymology, Pancreatic Elastase, Peptide Fragments, genetics, Seeds, Sequence Alignment, Serine Proteinase Inhibitors, chemistry, isolation & purification, pharmacology, Solanum tuberosum, Subtilisins, Trypsin, metabolism

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          A 7514-Da chymotrypsin inhibitor was isolated from the seed extract of Momordica cochinchinensis (Family Cucurbitaceae) by chromatography on chymotrypsin-Sepharose 4B and subsequently by C18 reversed-phase HPLC. This inhibitor, named MCoCl, possessed remarkable thermostability and was stable from pH 2 to 12. MCoCl also inhibited subtilisin, but had at least 50-fold lower inhibitory activity towards trypsin and elastase. Amino acid sequencing of a peptide fragment of MCoCl revealed a sequence of 23 amino acids. Comparison of this sequence and the molecular mass with those of other protease inhibitors suggests that MCoCl belongs to the potato I inhibitor family.

          Related collections

          Author and article information

          Journal
          15101561
          10.1515/BC.2004.037

          Comments

          Comment on this article