| Tartalom: |
http://real.mtak.hu/10029/ |
| Archívum: |
MTA Könyvtár |
| Gyűjtemény: |
Status = Submitted
Type = Article
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| Cím: |
Biochemical characterization of Acacia schweinfurthii serine
proteinase inhibitor
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| Létrehozó: |
Odei-Addo, Frank
Frost, Carminita
Smith, Nanette
Ogawa, Tomohisa
Muramoto, Koji
Gráf, László
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| Dátum: |
2013
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| Téma: |
Q1 Science (General) / természettudomány általában
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| Tartalmi leírás: |
One of the many control mechanisms of serine proteinases is their specific inhibition by protein
proteinase inhibitors. An extract of Acacia schweinfurthii was screened for potential serine
proteinase inhibition. It was successfully purified to homogeneity by precipitating with 80%
(v/v) acetone and sequential chromatographic steps, including ion-exchange, affinity purifica-
Q2 tion and RP-HPLC. Reducing SDS-PAGE conditions revealed an inhibitor (ASTI) consisting of two
polypeptide chains A and B of approximate molecular weights of 16 and 10 kDa, respectively,
and under non-reducing conditions, 26 kDa was observed. The inhibitor was shown to inhibit
bovine trypsin (Ki of 3.45 nM) at an approximate molar ratio of inhibitor: trypsin (1:1). The A- and
B-chains revealed complete sequences of 140 and 40 amino acid residues, respectively.
Sequence similarity (70%) was reported between ASTI A-chain and ACTI A-chain (Acacia
confusa) using the ClustalW. The B-chain produced a 76% sequence similarity between ASTI and
Leucaena leucocephala trypsin inhibitor.
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| Típus: |
Article
PeerReviewed
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| Formátum: |
text
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| Azonosító: |
Odei-Addo, Frank and Frost, Carminita and Smith, Nanette and Ogawa, Tomohisa and Muramoto, Koji and Gráf, László (2013) Biochemical characterization of Acacia schweinfurthii serine proteinase inhibitor. Journal of Enzyme Inhibition and Medicinal Chemistry (1-6). pp. 341-348. ISSN 1475-6366 (print), 1475-6374 (electronic) (Submitted)
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