鸽蛋清溶菌酶。纯化、结构及酶学特性

Pigeon egg white lysozyme. Purification, structural and enzymic characterization.

作者信息

Gavilanes J G, de Buitrago G G, del Pozo A M, Pérez-Castells R, Rodríguez R

出版信息

Int J Pept Protein Res. 1982 Sep;20(3):238-45.

Abstract

Lysozyme from pigeon egg white has been purified by ion exchange chromatography and gel filtration. The overall yield of the purification procedure is 65%. The specific activity of the enzyme is 15 000 units/mg. The influence of pH and ionic strength on the lytic activity of the protein, as well as its thermal stability, have been studied. The molecular weight, secondary structure estimation, amino acid composition, NH2- and COOH-terminal sequence of the protein are also reported. The pigeon enzyme has been classified as a chicken type lysozyme (lysozyme c) according to the obtained results.

摘要

鸽蛋清溶菌酶已通过离子交换色谱法和凝胶过滤法进行了纯化。纯化过程的总产率为65%。该酶的比活性为15000单位/毫克。研究了pH值和离子强度对该蛋白质溶菌活性的影响及其热稳定性。还报道了该蛋白质的分子量、二级结构评估、氨基酸组成、氨基末端和羧基末端序列。根据所得结果，该鸽酶已被归类为鸡型溶菌酶（溶菌酶c）。