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Difference-spectrophotometry of the interaction of cycloheptaamylose with saccharifying alpha-amylase from Bacillus subtilis.

作者信息

Onishi M, Hatano H, Hiromi K

出版信息

J Biochem. 1973 Sep;74(3):519-24. doi: 10.1093/oxfordjournals.jbchem.a130272.

DOI:10.1093/oxfordjournals.jbchem.a130272
PMID:4202121
Abstract
摘要

相似文献

1
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.
2
The effects of chemical modification by N-bromosuccinimide of saccharifying alpha-amylase from Bacillus subtilis on various substrates.N-溴代琥珀酰亚胺对枯草芽孢杆菌糖化α-淀粉酶进行化学修饰后对各种底物的影响。
J Biochem. 1974 Apr;75(4):767-77. doi: 10.1093/oxfordjournals.jbchem.a130449.
3
The number of subsites in the active site of saccharifying alpha-amylase from Bacillus subtilis.枯草芽孢杆菌糖化α-淀粉酶活性位点中的亚位点数量。
J Biochem. 1974 Sep;76(3):475-9. doi: 10.1093/oxfordjournals.jbchem.a130591.
4
Tryptophan residues of saccharifying alpha-amylase from Bacillus subtilis. A kinetic discrimination of states of tryptophan residues using N-bromosuccinimide.枯草芽孢杆菌糖化α-淀粉酶的色氨酸残基。使用N-溴代琥珀酰亚胺对色氨酸残基状态进行动力学区分。
J Biochem. 1978 May;83(5):1503-10. doi: 10.1093/oxfordjournals.jbchem.a132060.
5
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
J Biochem. 1970 Dec;68(6):933-6. doi: 10.1093/oxfordjournals.jbchem.a129433.
6
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.枯草芽孢杆菌糖化α-淀粉酶催化水解苯基α-麦芽糖苷的动力学及机制。II. 苯酚、苯基α-葡萄糖苷和麦芽三糖生成速率对底物浓度的依赖性。
J Biochem. 1969 May;65(5):741-50. doi: 10.1093/oxfordjournals.jbchem.a129072.
7
The characteristic action patterns of crystalline bacterial saccharifying alpha-amylase independent of its microheterogeneity.结晶型细菌糖化α-淀粉酶的特征性作用模式与其微观不均一性无关。
J Biochem. 1973 Dec;74(6):1267-70. doi: 10.1093/oxfordjournals.jbchem.a130355.
8
Kinetics and mechanism of hydrolysis of phenyl alpha-maltoside by saccharifying alpha-amylase of Bacillus subtilis. I. Formation of maltotriose in the course of hydrolysis.枯草芽孢杆菌糖化α-淀粉酶催化水解苯基α-麦芽糖苷的动力学及机制。I. 水解过程中麦芽三糖的形成
J Biochem. 1967 Oct;62(4):439-46. doi: 10.1093/oxfordjournals.jbchem.a128687.
9
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.
10
Regeneration of the native three-dimensional structure of Bacillus subtilis alpha-amylase and its formation in biological systems.枯草芽孢杆菌α-淀粉酶天然三维结构的再生及其在生物系统中的形成
J Biochem. 1968 Sep;64(3):283-92. doi: 10.1093/oxfordjournals.jbchem.a128894.

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Dihydrotanshinone I inhibits ovarian cancer cell proliferation and migration by transcriptional repression of PIK3CA gene.二氢丹参酮 I 通过转录抑制 PIK3CA 基因抑制卵巢癌细胞增殖和迁移。
J Cell Mol Med. 2020 Oct;24(19):11177-11187. doi: 10.1111/jcmm.15660. Epub 2020 Aug 29.
2
Studies on the active center of pancreatic amylase. I. Binding of beta-cyclodextrin.胰腺淀粉酶活性中心的研究。I. β-环糊精的结合
Mol Cell Biochem. 1974 Oct 30;4(3):205-9. doi: 10.1007/BF01731482.