4-碘乙酰氨基水杨酸与谷氨酸脱氢酶反应的位点。
The site at which 4-iodoacetamidosalicylate reacts with glutamate dehydrogenases.
作者信息
Holbrook J J, Roberts P A, Wallis R B
出版信息
Biochem J. 1973 May;133(1):165-71. doi: 10.1042/bj1330165.
Abstract
- Bovine, porcine and chicken liver glutamate dehydrogenases were irreversibly inhibited by a tenfold excess of radioactive 4-iodoacetamidosalicylic acid at pH7.5. 2. Inhibition was accompanied by the covalent incorporation of 1.1 mol of labelled inhibitor/mol of polypeptide chain. Acid hydrolysis yielded N(epsilon)-carboxymethyl-lysine as the sole labelled amino acid. No labelled S-carboxymethylcysteine was recovered from the bovine or porcine enzymes. 3. The labelled bovine enzyme was hydrolysed with trypsin. The radioactivity was found at lysine-126 in a peptide comprising residues 119-130 of the sequence. 4. The amino acid compositions of the tryptic peptides containing labelled lysine from the porcine and chicken enzymes were similar to that of the bovine peptide.
摘要
- 在pH7.5条件下，过量10倍的放射性4-碘乙酰氨基水杨酸可使牛、猪和鸡肝脏的谷氨酸脱氢酶受到不可逆抑制。2. 抑制作用伴随着每摩尔多肽链共价结合1.1摩尔标记抑制剂。酸水解产生N（ε）-羧甲基赖氨酸作为唯一的标记氨基酸。从牛或猪的酶中未回收标记的S-羧甲基半胱氨酸。3. 用胰蛋白酶水解标记的牛酶。在包含序列119-130位残基的肽段中的赖氨酸-126处发现放射性。4. 来自猪和鸡酶的含标记赖氨酸的胰蛋白酶肽段的氨基酸组成与牛肽段相似。
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本文引用的文献
1
Peptide separation by two-dimensional chromatography and electrophoresis.
J Biol Chem. 1959 Nov;234:2897-900.
2
[THE AMINE ACID COMPOSITION OF GLUTAMIC ACID DEHYDROGENASE FROM BEEF LIVER].
Biochem Z. 1964 Sep 28;340:421-35.
3
THE AMINO ACID SEQUENCE OF PSEUDOMONAS CYTOCHROME C-551.
Biochem J. 1963 Nov;89(2):349-78. doi: 10.1042/bj0890349.
4
Alkylation and identification of the histidine residues at the active site of ribonuclease.
J Biol Chem. 1963 Jul;238:2413-9.
5
The nature of the amino acid residues involved in the inactivation of ribonuclease by iodoacetate.
J Biol Chem. 1959 Jul;234(7):1754-60.
6
A peptide containing a reactive lysyl group from ox liver glutamate dehydrogenase.
Biochem J. 1969 Mar;111(5):689-94. doi: 10.1042/bj1110689.
7
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Eur J Biochem. 1970 Sep;15(3):555-61. doi: 10.1111/j.1432-1033.1970.tb01040.x.
8
Bovine liver flutamate dehydrogenase. Sequence of a hexadecapeptide containing a lysyl residue reactive with pyridoxal 5'-phosphate.
J Biol Chem. 1970 May 25;245(10):2622-6.
9
Glutamate dehydrogenase: amino-acid sequence of the bovine enzyme and comparison with that from chicken liver.
Proc Natl Acad Sci U S A. 1972 Jun;69(6):1380-3. doi: 10.1073/pnas.69.6.1380.
10
Purification and kinetic characteristics of dogfish liver glutamate dehydrogenase.
J Biol Chem. 1967 Apr 10;242(7):1383-90.
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