Detection of enzyme-bound intermediates by cross-saturation in nuclear magnetic resonance spectroscopy; an investigation of the papain–N-benzoylaminoacetaldehyde complex
Detection of enzyme-bound intermediates by cross-saturation in nuclear magnetic resonance spectroscopy; an investigation of the papain–N-benzoylaminoacetaldehyde complex
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通过核磁共振波谱交叉饱和检测酶结合中间体；木瓜蛋白酶-N-苯甲酰氨基乙醛复合物的研究
DOI：
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发表时间：
1977
期刊：
影响因子：
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通讯作者：
D. Nurse
中科院分区：
文献类型：
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作者：
P. Clark;G. Lowe;D. Nurse
甲半硫缩醛之间形成的活性位点硫醇的蛋白水解酶木瓜蛋白酶，和抑制剂N-苯甲酰氨基乙醛，已被检测到的双共振实验中，磁化之间转移的酶结合和自由的抑制剂。
A hemithioacetal formed between the active site thiol of the proteolytic enzyme papain, and the inhibitor N-benzoylaminoacetaldehyde, has been detected by a double resonance experiment in which magnetisation is transferred between the enzyme-bound and free inhibitor.