通过酪氨酸残基反应使谷氨酸脱氢酶脱敏。
Desensitization of glutamate dehydrogenase by reaction of tyrosne residues.
作者信息
Price N C, Radda G K
出版信息
Biochem J. 1969 Sep;114(2):419-27. doi: 10.1042/bj1140419.
Abstract
- The reaction of glutamate dehydrogenase with N-acetylimidazole and with tetranitromethane leads to modification of tyrosine residues. 2. Modification of 1 tyrosine residue/subunit does not affect the enzymic activity but decreases the response of the enzyme to the allosteric inhibitor, GTP. 3. The physical properties of the enzyme (sedimentation coefficient and optical rotatory dispersion) remain unaltered. 4. GTP partially protects against desensitization. 5. The diminished responses of the modified enzymes to GTP are also detected by using the fluorescence of 1-anilinonaphthalene-8-sulphonate as a conformational probe. 6. Difficulties that generally arise in chemical modifications from inhomogeneous distributions of products are discussed.
摘要
- 谷氨酸脱氢酶与N - 乙酰咪唑以及与四硝基甲烷的反应会导致酪氨酸残基的修饰。2. 每个亚基修饰1个酪氨酸残基不会影响酶活性，但会降低酶对变构抑制剂GTP的反应。3. 酶的物理性质（沉降系数和旋光色散）保持不变。4. GTP可部分防止脱敏。5. 通过使用1 - 苯胺基萘 - 8 - 磺酸盐的荧光作为构象探针，也能检测到修饰后的酶对GTP反应的减弱。6. 讨论了化学修饰中因产物分布不均一而普遍出现的困难。
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本文引用的文献
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THE REVERSAL BY ORGANIC MERCURIALS OF "ALLOSTERIC" CHANGES IN GLUTAMATE DEHYDROGENASE.有机汞对谷氨酸脱氢酶“变构”变化的逆转作用
J Biol Chem. 1965 Feb;240:668-73.
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3
GLUTAMATE DEHYDROGENASE. V. THE RELATION OF ENZYME STRUCTURE TO THE CATALYTIC FUNCTION.谷氨酸脱氢酶。五、酶结构与催化功能的关系。
J Biol Chem. 1963 Oct;238:3286-99.
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REACTIONS OF CYANURIC HALIDES WITH PROTEINS. I. BOUND TYROSINE RESIDUES OF INSULIN AND LYSOZYME AS IDENTIFIED WITH CYANURIC FLUORIDE.三聚氰酰卤与蛋白质的反应。I. 用三聚氰酰氟鉴定胰岛素和溶菌酶中结合的酪氨酸残基。
Biochim Biophys Acta. 1963 Sep 10;74:678-87. doi: 10.1016/0006-3002(63)91419-7.
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J Mol Biol. 1963 Apr;6:306-29. doi: 10.1016/s0022-2836(63)80091-1.
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A simple ultraviolet spectrophotometric method for the determination of protein.一种测定蛋白质的简易紫外分光光度法。
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Biochemistry. 1966 Sep;5(9):2893-900. doi: 10.1021/bi00873a017.
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