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2. Detection of human urinary alpha-amylase encoded by the AMY2B gene using a fluorogenic substrate, FG5P. Omichi K, Hase S. J Biochem; 1992 Sep; 112(3):303-5. PubMed ID: 1429515 [Abstract] [Full Text] [Related]
4. Inspection of active sites of human salivary alpha-amylase isozymes by means of non-reducing-end substituted maltooligosaccharides with 2-pyridylamino residue. Omichi K, Ikenaka T. J Biochem; 1986 Apr; 99(4):1245-52. PubMed ID: 3486866 [Abstract] [Full Text] [Related]
5. 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 [Abstract] [Full Text] [Related]
6. Preparation of non-reducing-end substituted p-nitrophenyl alpha-maltopentaoside (FG5P) as a substrate for a coupled enzymatic assay for alpha-amylases. Omichi K, Ikenaka T. J Biochem; 1985 Apr; 97(4):977-82. PubMed ID: 3161874 [Abstract] [Full Text] [Related]
7. Mechanism of action of human pancreatic and salivary alpha-amylase on 4,6-ethylidene-alpha-4-nitrophenyl-maltoheptaoside substrate. Hägele EO, Kratzer M, Schaich E, Rauscher E. Clin Chem; 1989 Jan; 35(1):188-9. PubMed ID: 2783397 [No Abstract] [Full Text] [Related]
8. Alpha-amylase assay with use of a benzyl derivative of p-nitrophenyl alpha-maltopentaoside, BG5P. Satomura S, Sakata Y, Omichi K, Ikenaka T. Clin Chim Acta; 1988 Jun 15; 174(3):315-23. PubMed ID: 3134147 [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 15; 20(8):581-6. PubMed ID: 6183388 [Abstract] [Full Text] [Related]
14. Fluorometric rate assay of alpha-amylase using an intramolecularly-quenched fluorescent substrate (FG5P). Omichi K, Ikenaka T. J Biochem; 1986 Jan 15; 99(1):291-4. PubMed ID: 3485629 [Abstract] [Full Text] [Related]
15. 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 [Abstract] [Full Text] [Related]
16. Measurement of cyclomaltodextrin glucanotransferase activity by high-performance liquid chromatography using a fluorogenic substrate. Satomura S, Omichi K, Ikenaka T. Anal Biochem; 1986 May 01; 154(2):449-53. PubMed ID: 2942054 [Abstract] [Full Text] [Related]
17. 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 05; 298(3):237-42. PubMed ID: 9090818 [Abstract] [Full Text] [Related]
18. 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 [Abstract] [Full Text] [Related]