Autor: |
Nguyen, Thi, Jung, Sun-Hwa, Lee, Sun, Ryu, Hwa-Ja, Kang, Hee-Kyoung, Moon, Young-Hwan, Kim, Young-Min, Kimura, Atsuo, Kim, Doman |
Předmět: |
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Zdroj: |
Biotechnology & Bioprocess Engineering; Oct2012, Vol. 17 Issue 5, p966-971, 6p |
Abstrakt: |
Human intestinal maltase (HMA) is an α-glucosidase responsible for the hydrolysis of α-1,4-linkages from the non-reducing end of malto-oligosaccharides. HMA has become an important target in the treatment of type-2 diabetes. In this study, epigallocatechin gallate (EGCG) and EGCG glucoside (EGCG-G1) were identified as inhibitors of HMA by an in vitro assay with IC of 20 ± 1.0 and 31.5 ± 1.0 μM, respectively. A Lineweaver-Burk plot confirmed that EGCG and EGCG-G1 were competitive inhibitors of maltose substrate against HMA and inhibition kinetic constants ( K) calculated from a Dixon plot were 5.93 ± 0.26 and 7.88 ± 0.57 μM, respectively. Both EGCG and EGCG-G1 bound to the active site of HMA with numerous hydrophobic and hydrogen bond interactions. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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