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297 related items for PubMed ID: 11168426

  • 1. Mechanism of porcine pancreatic alpha-amylase. Inhibition of amylose and maltopentaose hydrolysis by alpha-, beta- and gamma-cyclodextrins.
    Koukiekolo R, Desseaux V, Moreau Y, Marchis-Mouren G, Santimone M.
    Eur J Biochem; 2001 Feb; 268(3):841-8. PubMed ID: 11168426
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  • 3. The mechanism of porcine pancreatic alpha-amylase. Kinetic evidence for two additional carbohydrate-binding sites.
    Alkazaz M, Desseaux V, Marchis-Mouren G, Payan F, Forest E, Santimone M.
    Eur J Biochem; 1996 Nov 01; 241(3):787-96. PubMed ID: 8944767
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  • 4. Porcine pancreatic alpha-amylase inhibition by the kidney bean (Phaseolus vulgaris) inhibitor (alpha-AI1) and structural changes in the alpha-amylase inhibitor complex.
    Santimone M, Koukiekolo R, Moreau Y, Le Berre V, Rougé P, Marchis-Mouren G, Desseaux V.
    Biochim Biophys Acta; 2004 Feb 12; 1696(2):181-90. PubMed ID: 14871659
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  • 5. The mechanism of porcine pancreatic alpha-amylase. Inhibition of maltopentaose hydrolysis by acarbose, maltose and maltotriose.
    Al Kazaz M, Desseaux V, Marchis-Mouren G, Prodanov E, Santimone M.
    Eur J Biochem; 1998 Feb 15; 252(1):100-7. PubMed ID: 9523717
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  • 7. On porcine pancreatic alpha-amylase action: kinetic evidence for the binding of two maltooligosaccharide molecules (maltose, maltotriose and o-nitrophenylmaltoside) by inhibition studies. Correlation with the five-subsite energy profile.
    Seigner C, Prodanov E, Marchis-Mouren G.
    Eur J Biochem; 1985 Apr 01; 148(1):161-8. PubMed ID: 3872211
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  • 8. Inhibition of reduced DP18-maltodextrin and amylose hydrolysis by acarbose: kinetic studies.
    Alkazaz M, Desseaux V, Prodanov E, Marchis-Mouren G, Santimone M.
    Int J Biol Macromol; 1997 Aug 01; 21(1-2):97-101. PubMed ID: 9283022
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  • 10. Kinetic difference between hydrolyses of gamma-cyclodextrin by human salivary and pancreatic alpha-amylases.
    Marshall JJ, Miwa I.
    Biochim Biophys Acta; 1981 Sep 15; 661(1):142-7. PubMed ID: 6170334
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  • 14. Effect of pressure on the mechanism of hydrolysis of maltotetraose, maltopentaose, and maltohexose catalyzed by porcine pancreatic alpha-amylase.
    Matsumoto T, Makimoto S, Taniguchi Y.
    Biochim Biophys Acta; 1997 Dec 05; 1343(2):243-50. PubMed ID: 9434115
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  • 17. Kinetic investigation of a new inhibitor for human salivary alpha-amylase.
    Kandra L, Zajácz A, Remenyik J, Gyémánt G.
    Biochem Biophys Res Commun; 2005 Sep 02; 334(3):824-8. PubMed ID: 16023996
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  • 18. The effect of substrate modification on binding of porcine pancreatic alpha amylase: hydrolysis of modified amylose containing D-allose residues.
    Braun PJ, French D, Robyt JF.
    Carbohydr Res; 1985 Sep 01; 141(2):265-71. PubMed ID: 3877569
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  • 20. Effect of maltotriitol on the action pattern of porcine pancreatic alpha-amylase using amylose as a substrate.
    Kondo H, Nakatani H, Hiromi K.
    Carbohydr Res; 1990 Sep 30; 206(1):161-6. PubMed ID: 2081342
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