Bifunctional inhibitor of α-amylase/trypsin from wheat grain
A trypsin inhibitor, isolated from whole-wheat grain (Triticum aestivum L.) by the method of biospecific chromatography on trypsin-Sepharose, was potent in inhibiting human salivary alpha -amylase. The bifunctional alpha -amylase/trypsin inhibitor was characterized by a narrow specificity for other...
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| Veröffentlicht in: | Applied biochemistry and microbiology 2007-07, Vol.43 (4), p.379-382 |
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| container_title | Applied biochemistry and microbiology |
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| creator | Islamov, R. A. Fursov, O. V. |
| description | A trypsin inhibitor, isolated from whole-wheat grain (Triticum aestivum L.) by the method of biospecific chromatography on trypsin-Sepharose, was potent in inhibiting human salivary alpha -amylase. The bifunctional alpha -amylase/trypsin inhibitor was characterized by a narrow specificity for other alpha -amylases and proteinases. The high thermostability of the inhibitor was lost in the presence of SH group-reducing agents. The inhibitor-trypsin complex retained its activity against alpha -amylase. The inhibitor- alpha -amylase complex was active against trypsin. Studies of the enzyme kinetics demonstrated that the inhibition of alpha -amylase and trypsin was noncompetitive. Our results suggest the existence of two independent active sites responsible for the interaction with the enzymes. |
| doi_str_mv | 10.1134/S0003683807040035 |
| format | Article |
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A. ; Fursov, O. V.</creator><creatorcontrib>Islamov, R. A. ; Fursov, O. V.</creatorcontrib><description>A trypsin inhibitor, isolated from whole-wheat grain (Triticum aestivum L.) by the method of biospecific chromatography on trypsin-Sepharose, was potent in inhibiting human salivary alpha -amylase. The bifunctional alpha -amylase/trypsin inhibitor was characterized by a narrow specificity for other alpha -amylases and proteinases. The high thermostability of the inhibitor was lost in the presence of SH group-reducing agents. The inhibitor-trypsin complex retained its activity against alpha -amylase. The inhibitor- alpha -amylase complex was active against trypsin. Studies of the enzyme kinetics demonstrated that the inhibition of alpha -amylase and trypsin was noncompetitive. Our results suggest the existence of two independent active sites responsible for the interaction with the enzymes.</description><identifier>ISSN: 0003-6838</identifier><identifier>EISSN: 1608-3024</identifier><identifier>DOI: 10.1134/S0003683807040035</identifier><language>eng</language><subject>Triticum aestivum</subject><ispartof>Applied biochemistry and microbiology, 2007-07, Vol.43 (4), p.379-382</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c276t-354c982283f9c668c1bb2bb189ac3f3cfa74210e36dcfc1ad718bd8a65a323c73</citedby><cites>FETCH-LOGICAL-c276t-354c982283f9c668c1bb2bb189ac3f3cfa74210e36dcfc1ad718bd8a65a323c73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Islamov, R. A.</creatorcontrib><creatorcontrib>Fursov, O. V.</creatorcontrib><title>Bifunctional inhibitor of α-amylase/trypsin from wheat grain</title><title>Applied biochemistry and microbiology</title><description>A trypsin inhibitor, isolated from whole-wheat grain (Triticum aestivum L.) by the method of biospecific chromatography on trypsin-Sepharose, was potent in inhibiting human salivary alpha -amylase. The bifunctional alpha -amylase/trypsin inhibitor was characterized by a narrow specificity for other alpha -amylases and proteinases. The high thermostability of the inhibitor was lost in the presence of SH group-reducing agents. The inhibitor-trypsin complex retained its activity against alpha -amylase. The inhibitor- alpha -amylase complex was active against trypsin. Studies of the enzyme kinetics demonstrated that the inhibition of alpha -amylase and trypsin was noncompetitive. 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Studies of the enzyme kinetics demonstrated that the inhibition of alpha -amylase and trypsin was noncompetitive. Our results suggest the existence of two independent active sites responsible for the interaction with the enzymes.</abstract><doi>10.1134/S0003683807040035</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-6838 |
| ispartof | Applied biochemistry and microbiology, 2007-07, Vol.43 (4), p.379-382 |
| issn | 0003-6838 1608-3024 |
| language | eng |
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| subjects | Triticum aestivum |
| title | Bifunctional inhibitor of α-amylase/trypsin from wheat grain |
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