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[Active site of ATP: guanidine phosphotransferases. I. Reaction of the essential epsilon-NH2 lysine groups with 1-dimethylaminonapthalene-5-sulphonyl chloride].

作者信息

Kassab R, Roustan C, Pradel L A

出版信息

Biochim Biophys Acta. 1968 Oct 8;167(2):308-16. doi: 10.1016/0005-2744(68)90210-6.

DOI:10.1016/0005-2744(68)90210-6
PMID:5729946
Abstract
摘要

相似文献

1
[Active site of ATP: guanidine phosphotransferases. I. Reaction of the essential epsilon-NH2 lysine groups with 1-dimethylaminonapthalene-5-sulphonyl chloride].
Biochim Biophys Acta. 1968 Oct 8;167(2):308-16. doi: 10.1016/0005-2744(68)90210-6.
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THE DISTRIBUTION OF GUANIDINE-ADENOSINE TRIPHOSPHATE PHOSPHOTRANSFERASES AND ADENOSINE TRIPHOSPHATASE IN ANIMALS FROM SEVERAL PHYLA.几种动物门中胍基 - 三磷酸腺苷磷酸转移酶和三磷酸腺苷酶的分布
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Biochem J. 1969 Mar;111(5):797-8. doi: 10.1042/bj1110797.

引用本文的文献

1
Reactivation kinetics of guanidine hydrochloride-denatured creatine kinase measured using the substrate reaction.使用底物反应测定盐酸胍变性肌酸激酶的复活动力学。
J Protein Chem. 2001 Jan;20(1):67-72. doi: 10.1023/a:1011046814606.
2
Effect of Mg2+ during reactivation and refolding of guanidine hydrochloride-denatured creatine kinase.Mg2+对盐酸胍变性的肌酸激酶复性和重折叠的影响。
J Protein Chem. 2000 Apr;19(3):193-8. doi: 10.1023/a:1007003703087.
3
Creatine kinase: essential arginine residues at the nucleotide binding site identified by chemical modification and high-resolution tandem mass spectrometry.
肌酸激酶：通过化学修饰和高分辨率串联质谱法鉴定出的核苷酸结合位点处的必需精氨酸残基。
Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3362-5. doi: 10.1073/pnas.95.7.3362.
4
Conformational changes at the active site of creatine kinase at low concentrations of guanidinium chloride.低浓度氯化胍作用下肌酸激酶活性位点的构象变化
Biochem J. 1993 Apr 1;291 ( Pt 1)(Pt 1):103-7. doi: 10.1042/bj2910103.
5
Conformational heterogeneity of creatine kinase determined from phase resolved fluorometry.通过相分辨荧光法测定肌酸激酶的构象异质性。
Biophys J. 1991 Mar;59(3):590-7. doi: 10.1016/S0006-3495(91)82274-3.
6
The reaction of rabbit muscle creatine kinase with diethyl pyrocarbonate.兔肌肉肌酸激酶与焦碳酸二乙酯的反应
Biochem J. 1979 Aug 1;181(2):467-75. doi: 10.1042/bj1810467.