人溶菌酶的化学修饰。酪氨酸的乙酰化和硝化。 - Suppr

Chemical modification of human lysozyme. Acetylation and nitration of tyrosine.

作者信息

Fawcett R I, Limbird T J, Oliver S L, Borders C L

出版信息

Can J Biochem. 1971 Jul;49(7):816-21. doi: 10.1139/o71-115.

DOI:10.1139/o71-115

PMID:5557892

Abstract

摘要

相似文献

Chemical modification of human lysozyme. Acetylation and nitration of tyrosine.

Can J Biochem. 1971 Jul;49(7):816-21. doi: 10.1139/o71-115.

Modification of the amino group of isoleucine-16 in chymotrypsin with retention of activity.

Biochem Biophys Res Commun. 1971 May 7;43(3):510-5. doi: 10.1016/0006-291x(71)90643-7.

Reaction of N-bromosuccinimide with lysozyme.

Biochim Biophys Acta. 1967 Dec 12;147(3):462-72. doi: 10.1016/0005-2795(67)90006-2.

The nature of amino acid side chains which are critical for the activity of lysozyme.

Biochemistry. 1969 Feb;8(2):700-12. doi: 10.1021/bi00830a036.

Further chemical modification studies on concanavalin A, the carbohydrate binding protein of the jack bean.

Biochim Biophys Acta. 1972 Jul 21;271(2):388-99. doi: 10.1016/0005-2795(72)90214-0.

Modification of lysine and arginine residues of lysozyme and the effect on enzymatic activity.

Biochim Biophys Acta. 1969 Apr 22;178(2):306-17. doi: 10.1016/0005-2744(69)90398-2.

Specific O-acylation of hydroxylamino acids in presence of free amino groups.

Biochim Biophys Acta. 1972 Mar 15;263(1):7-13. doi: 10.1016/0005-2795(72)90154-7.

C-acylation of the tryptophan indole ring and its usefulness in protein chemistry.

Biochim Biophys Acta. 1972 Dec 28;285(2):269-78. doi: 10.1016/0005-2795(72)90310-8.

Metal-combining properties of human lactoferrin. The effect of nitration of lactoferrin with tetranitromethane.

Eur J Biochem. 1973 Jun;35(2):366-71. doi: 10.1111/j.1432-1033.1973.tb02848.x.

Chemical modification of tyrosyl residues of hen egg-white lysozyme by diisopropylphosphorofluoridate.

J Biochem. 1971 Apr;69(4):725-37. doi: 10.1093/oxfordjournals.jbchem.a129521.

引用本文的文献

Preferential nitration with tetranitromethane of a specific tyrosine residue in penicillinase from Staphylococcus aureus PCl. Evidence that the preferentially nitrated residue is not part of the active site but that loss of activity is due to intermolecular cross-linking.

Biochem J. 1978 Feb 1;169(2):381-8. doi: 10.1042/bj1690381.

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Chemical modification of human lysozyme. Acetylation and nitration of tyrosine.

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Chemical modification of human lysozyme. Acetylation and nitration of tyrosine.

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