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Difference spectrophotometric study of interaction between maltose and saccharifying alpha-amylase from Bacillus subtilis.

作者信息

Onishi M

出版信息

J Biochem. 1970 Dec;68(6):933-6. doi: 10.1093/oxfordjournals.jbchem.a129433.

DOI:10.1093/oxfordjournals.jbchem.a129433
PMID:4993290
Abstract
摘要

相似文献

1
Difference spectrophotometric study of interaction between maltose and saccharifying alpha-amylase from Bacillus subtilis.麦芽糖与枯草芽孢杆菌糖化α-淀粉酶相互作用的差示分光光度法研究
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J Biochem. 1969 Jul;66(1):63-7. doi: 10.1093/oxfordjournals.jbchem.a129121.
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Substituent effect on the hydrolyses of phenyl -maltosides catalyzed by saccharifying -amylase from Bacillus subtilis.枯草芽孢杆菌糖化型α-淀粉酶催化的苯基麦芽糖苷水解中的取代基效应
J Biochem. 1971 Oct;70(4):595-601. doi: 10.1093/oxfordjournals.jbchem.a129676.
5
Reaction mechanism of saccharifying alpha-amylase from B. subtilis with maltose as a substrate.以麦芽糖为底物时枯草芽孢杆菌糖化型α-淀粉酶的反应机制
J Biochem. 1977 Aug;82(2):417-27.
6
Substrate concentration dependence of the rate of maltose hydrolysis by saccharifying alpha-amylase from B. subtilis.枯草芽孢杆菌糖化型α-淀粉酶催化麦芽糖水解速率对底物浓度的依赖性
J Biochem. 1975 May;77(5):965-8. doi: 10.1093/oxfordjournals.jbchem.a130821.
7
Kinetic studies by stopped-flow method of hydrolysis of 0-nitrophenyl alpha-maltoside catalyzed by saccharifying alpha-amylase from Bacillus subtilis.利用停流法对枯草芽孢杆菌糖化α-淀粉酶催化水解对硝基苯基α-麦芽糖苷进行动力学研究。
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Kinetics and mechanism of transfer action of saccharifying alpha-amylase of Bacillus subtilis. Maltose--phenyl alpha-glucoside system.枯草芽孢杆菌糖化α-淀粉酶转糖基作用的动力学与机制。麦芽糖 - 苯基α-葡萄糖苷体系
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Threshold in a single enzyme reaction system. Reaction of maltose catalyzed by saccharifying alpha-amylase from B. subtilis.单一酶反应体系中的阈值。枯草芽孢杆菌糖化α-淀粉酶催化麦芽糖的反应。
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Difference-spectrophotometry of the interaction of cycloheptaamylose with saccharifying alpha-amylase from Bacillus subtilis.
J Biochem. 1973 Sep;74(3):519-24. doi: 10.1093/oxfordjournals.jbchem.a130272.