Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human mucous secretions contain a proteinase inhibitor which is produced locally and inhibits, besides trypsin and chymotrypsin, granulocytic elastase and cathepsin G as well as mast cell chymase and tryptase. The various inhibitors isolated from different sources (bronchial mucus, parotid secretion, seminal plasma, cervical mucus, etc.) and named accordingly (bronchial mucus inhibitor, BMI; human seminal inhibitor I, HUSI-I; cervical mucus inhibitors, CUSI; antileukoprotease, ALP; secretory leukocyte protease inhibitor, SLPI) proved to be identical or derived from a mature inhibitory protein encoded by a single gene of the human genom. Therefore, this inhibitor should be named mucus proteinase inhibitor, MPI. Such a neutral terminus would help to avoid misleading interpretations of already published data and also of the biological role of this inhibitory protein because the MPI may serve several and different physiological functions.
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PMID:Human mucus proteinase inhibitor (human MPI). Human seminal inhibitor I (HUSI-I), antileukoprotease (ALP), secretory leukocyte protease inhibitor (SLPI). 306 Jan 47

The proteinase inhibitor WSCI, active in inhibiting bacterial subtilisin and a number of animal chymotrypsins, was purified from endosperm of exaploid wheat (Triticum aestivum, c.v. San Pastore) by ion exchange chromatography and its complete amino acid sequence was established by automated Edman degradation. WSCI consists of a single polypeptide chain of 72 amino acid residues, has a molecular mass of 8126.3 Da and a pl of 5.8. The inhibition constants (Ki) for Bacillus licheniformis subtilisin and bovine pancreatic alpha-chymotrypsin are 3.92 x 10(-9) M and 7.24 x 10(-9) M, respectively. The inhibitor contains one methionine and of tryptophan residue and has a high content of essential amino acids (41 over a total of 72 residues), but no cysteines. The primary structure of WSCI shows high similarity with barley subtilisin-chymotrypsin isoinhibitors of the Cl-2 type and with maize subtilisinchymotrypsin inhibitor MPI. Significant degrees of similarity were also found between sequences of WSCI and of other members of the potato inhibitor I family of the serine proteinase inhibitors. The wheat inhibitor WSCI has a single reactive site (the peptide bond between methionyl-48 and glutamyl-49 residues) as identified by affinity chromatography and sequence analysis.
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PMID:Primary structure and reactive site of a novel wheat proteinase inhibitor of subtilisin and chymotrypsin. 1267 23