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Journal Abstract Search

157 related items for PubMed ID: 410799

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  • 4. Hydrolysis of phenyl beta-maltoside catalyzed by saccharifying alpha-amylase from Bacillus subtilis.
    Ishikura K, Nitta Y, Watanabe T.
    J Biochem; 1977 May; 81(5):1187-92. PubMed ID: 408329
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  • 7. Kinetics and mechanism of transfer action of saccharifying alpha-amylase of Bacillus subtilis. Maltose--phenyl alpha-glucoside system.
    Yoshida H, Hiromi K, Ono S.
    J Biochem; 1969 Aug; 66(2):183-90. PubMed ID: 4981458
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  • 8. [Molecular cloning of alpha-amylase gene from Bacillus megaterium and its expression in Bacillus subtilis].
    Lü XY, Jiang RZ, Wang GF.
    Yi Chuan Xue Bao; 1991 Aug; 18(2):185-92. PubMed ID: 1909533
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  • 9. Kinetics and mechanism of hydrolysis of phenyl alpha-maltos- ide by saccharifying alpha-amylase of Bacillus subtilis. II. Dependence of the rates of formation of phenol, phenyl alpha-glucoside and maltotriose on the substrate concentration.
    Yoshida H, Hiromi K, Ono S.
    J Biochem; 1969 May; 65(5):741-50. PubMed ID: 4979925
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  • 11. Allosteric behavior irrespective of conformational change of enzyme protein. Sigmoidal concentration dependence of rate of action of saccharifying alpha-amylase on maltose.
    Fujimori H, Ohnishi M, Sakoda M, Matsuno R, Hiromi K.
    FEBS Lett; 1976 Dec 31; 72(2):283-6. PubMed ID: 16386041
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  • 14. [Isolation and study of physico-chemical properties of alpha-amylase from Bacillus subtilis].
    Kostareva IA, Orlievskaia OV, Iurchenko VS, Ponomareva RB, Samsonov GV.
    Prikl Biokhim Mikrobiol; 1981 Dec 31; 17(3):430-5. PubMed ID: 6174969
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  • 16. Kinetic studies by stopped-flow method of hydrolysis of 0-nitrophenyl alpha-maltoside catalyzed by saccharifying alpha-amylase from Bacillus subtilis.
    Suetsugu N, Hiromi K, Ono S.
    J Biochem; 1971 Feb 31; 69(2):421-4. PubMed ID: 4994527
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  • 18. The number of subsites in the active site of saccharifying alpha-amylase from Bacillus subtilis.
    Shibaoka T, Miyano K, Watanabe T.
    J Biochem; 1974 Sep 31; 76(3):475-9. PubMed ID: 4215806
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