Thermal denaturation of native and cross-linked bacillus cereus 569/II β-lactamase I
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference18 articles.
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Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Characterization of covalently bound enzyme inhibitors as transition-state analogs by protein stability measurements: Phosphonate monoester inhibitors of .beta.-lactamase;Biochemistry;1994-01-11
2. Differential scanning calorimetric study of the thermal unfolding of .beta.-lactamase I from Bacillus cereus;Biochemistry;1992-07-21
3. Potentiation of thermal inactivation of glyceraldehyde-3-phosphate dehydrogenase by photodynamic treatment. A possible model for the synergistic interaction between photodynamic therapy and hyperthermia;Biochemical Journal;1991-06-01
4. Automated analysis of enzyme inactivation phenomena;Biochemical Pharmacology;1987-07
5. Inhibition of β-lactamase-I by 6-β-sulfonamidopenicillanic acid sulfones: Evidence for conformational change accompanying the inhibition process;Bioorganic Chemistry;1985-03
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