BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

123 related articles for article (PubMed ID: 8512936)

  • 1. Substrate recognition at the binding site in mammalian pancreatic alpha-amylases.
    Ishikawa K; Matsui I; Kobayashi S; Nakatani H; Honda K
    Biochemistry; 1993 Jun; 32(24):6259-65. PubMed ID: 8512936
    [TBL] [Abstract][Full Text] [Related]  

  • 2. The pH dependence of the action pattern in porcine pancreatic alpha-amylase-catalyzed reaction for maltooligosaccharide substrates.
    Ishikawa K; Matsui I; Honda K; Kobayashi S; Nakatani H
    Arch Biochem Biophys; 1991 Aug; 289(1):124-9. PubMed ID: 1898059
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Substrate-dependent shift of optimum pH in porcine pancreatic alpha-amylase-catalyzed reactions.
    Ishikawa K; Matsui I; Honda K; Nakatani H
    Biochemistry; 1990 Jul; 29(30):7119-23. PubMed ID: 2223766
    [TBL] [Abstract][Full Text] [Related]  

  • 4. 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; 1343(2):243-50. PubMed ID: 9434115
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Optimum pH control mechanism for porcine pancreatic alpha-amylase.
    Ishikawa K; Matsui I; Honda K
    Biosci Biotechnol Biochem; 1995 Jun; 59(6):1175-6. PubMed ID: 7613011
    [TBL] [Abstract][Full Text] [Related]  

  • 6. The effect of substrate modification on porcine pancreatic alpha-amylase subsite binding: hydrolysis of substrates containing 2-deoxy-D-glucose and 2-amino-2-deoxy-D-glucose.
    Braun PJ; French D; Robyt JF
    Arch Biochem Biophys; 1985 Oct; 242(1):231-9. PubMed ID: 2932056
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Actions of three human alpha-amylases expressed in yeast on modified substrates and the amino acid residues causing their different actions.
    Omichi K; Shiosaki K; Matsubara K; Ikenaka T
    J Biochem; 1989 Oct; 106(4):646-50. PubMed ID: 2691509
    [TBL] [Abstract][Full Text] [Related]  

  • 8. The determination of subsite binding energies of porcine pancreatic alpha-amylase by comparing hydrolytic activity towards substrates.
    Seigner C; Prodanov E; Marchis-Mouren G
    Biochim Biophys Acta; 1987 Jun; 913(2):200-9. PubMed ID: 3496119
    [TBL] [Abstract][Full Text] [Related]  

  • 9. 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; 141(2):265-71. PubMed ID: 3877569
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Porcine-pancreatic alpha amylase hydrolysis of substrates containing 6-deoxy-D-glucose and 6-deoxy-6-fluoro-D-glucose and the specificity of subsite binding.
    Braun PJ; French D; Robyt JF
    Carbohydr Res; 1985 Nov; 143():107-16. PubMed ID: 3878731
    [TBL] [Abstract][Full Text] [Related]  

  • 11. 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; 148(1):161-8. PubMed ID: 3872211
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Glycosylated salivary alpha-amylases are capable of maltotriose hydrolysis and glucose formation.
    Koyama I; Komine S; Yakushijin M; Hokari S; Komoda T
    Comp Biochem Physiol B Biochem Mol Biol; 2000 Aug; 126(4):553-60. PubMed ID: 11026667
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Action pattern of human pancreatic and salivary alpha-amylase on 1,4-alpha-D-nitrophenylmaltooligosaccharides. 1,4-alpha-D-nitrophenylmaltooligosaccharides as substrates of alpha-amylse, I.
    Wallenfels K; Laule G; Meltzer B
    J Clin Chem Clin Biochem; 1982 Aug; 20(8):581-6. PubMed ID: 6183388
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Effect of a p-nitro group of phenyl-maltooligosaccharide substrate on the change of action specificity of lysine-modified porcine pancreatic alpha-amylase.
    Yamashita H; Nakatani H; Tonomura B
    Biochem Mol Biol Int; 1995 Jan; 35(1):79-85. PubMed ID: 7735142
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Studies on the substrate specificity of alpha- and beta-amylase of Entamoeba histolytica.
    Werries E; Müller F
    Mol Biochem Parasitol; 1986 Feb; 18(2):211-21. PubMed ID: 2421162
    [TBL] [Abstract][Full Text] [Related]  

  • 16. 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
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Examination of aglycone-binding site of human salivary alpha-amylase by means of transglycosylation reactions.
    Omichi K; Hase S; Ikenaka T
    J Biochem; 1991 Mar; 109(3):410-5. PubMed ID: 1880127
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Subsite profile of the active center of porcine pancreatic alpha-amylase. Kinetic studies using maltooligosaccharides as substrates.
    Prodanov E; Seigner C; Marchis-Mouren G
    Biochem Biophys Res Commun; 1984 Jul; 122(1):75-81. PubMed ID: 6611158
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Action pattern of porcine pancreatic alpha-amylase on three different series of beta-maltooligosaccharide glycosides.
    Kandra L; Gyémánt G; Farkas E; Lipták A
    Carbohydr Res; 1997 Mar; 298(3):237-42. PubMed ID: 9090818
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Porcine pancreatic alpha-amylase hydrolysis of hydroxyethylated amylose and specificity of subsite binding.
    Chan Y; Braun PJ; French D; Robyt JF
    Biochemistry; 1984 Nov; 23(24):5795-800. PubMed ID: 6441594
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 7.