Primary Structure and Reactive Site of a NovelWheat Proteinase Inhibitor of Subtilisin andChymotrypsin
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| 024 | 7 | 0 | |a 10.1515/BC.2003.033 |2 doi |
| 035 | |a (NATIONALLICENCE)gruyter-10.1515/BC.2003.033 | ||
| 245 | 0 | 0 | |a Primary Structure and Reactive Site of a NovelWheat Proteinase Inhibitor of Subtilisin andChymotrypsin |h [Elektronische Daten] |c [E. Poerio, S. Di Gennaro, A. Di Maro, F. Farisei, P. Ferranti, A. Parente] |
| 520 | 3 | |a 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 pI of 5.8. The inhibition constants (K1) for Bacillus licheniformis subtilisin and bovine pancreatic α-chymotrypsin are 3.92×10 -9 M and 7.24×10 -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 CI-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. | |
| 540 | |a Copyright © 2003 by Walter de Gruyter GmbH & Co. KG | ||
| 690 | 7 | |a Biochemistry |2 nationallicence | |
| 690 | 7 | |a Molecular biology |2 nationallicence | |
| 690 | 7 | |a Cellular biology |2 nationallicence | |
| 700 | 1 | |a Poerio |D E. |4 aut | |
| 700 | 1 | |a Gennaro |D S. Di |4 aut | |
| 700 | 1 | |a Maro |D A. Di |4 aut | |
| 700 | 1 | |a Farisei |D F. |4 aut | |
| 700 | 1 | |a Ferranti |D P. |4 aut | |
| 700 | 1 | |a Parente |D A. |4 aut | |
| 773 | 0 | |t Biological Chemistry |d Walter de Gruyter |g 384/2(2003-02-20), 295-304 |x 1431-6730 |q 384:2<295 |1 2003 |2 384 |o bchm | |
| 856 | 4 | 0 | |u https://doi.org/10.1515/BC.2003.033 |q text/html |z Onlinezugriff via DOI |
| 908 | |D 1 |a research article |2 jats | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1515/BC.2003.033 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Poerio |D E. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Gennaro |D S. Di |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Maro |D A. Di |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Farisei |D F. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Ferranti |D P. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Parente |D A. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Biological Chemistry |d Walter de Gruyter |g 384/2(2003-02-20), 295-304 |x 1431-6730 |q 384:2<295 |1 2003 |2 384 |o bchm | ||
| 900 | 7 | |b CC0 |u http://creativecommons.org/publicdomain/zero/1.0 |2 nationallicence | |
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| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-gruyter | ||