ISOLATION AND CHARACTERIZATION OF HUMAN MILK LYSOZYME

被引：72

作者：

PARRY, RM

CHANDAN, RC

SHAHANI, KM

机构：

[1] Department of Food Science and Technology, University of Nebraska, Lincoln

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1969年 / 130卷 / 1-2期

关键词：

D O I：

10.1016/0003-9861(69)90009-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A modified technique for the isolation of human milk lysozyme (HML)4 4 Abbreviations used: HML, human milk lysozyme; EWL, egg-white lysozyme; BML, bovine milk lysozyme. is described. The method yielded a protein with a specific activity of 3.5 as compared to egg-white lysozyme's (EWL) value of 1.0. The isoelectric point was 10.5-11.0, slightly higher than that of EWL. The sedimentation velocity molecular weight was found to be 16,000 with a sc=o20.w of 2.19, D20.w of 11.92, and v̄ of 0.721 ml/g. The molecular weight by short-column sedimentation equilibrium was 15,000 ± 600. The amino acid analysis gave 123 ± 2 residues per mole, with a minimum molecular weight of 14,000. The enzyme also showed high thermal stability and a single pH optimum at 6.35. © 1969.

引用

页码：59 / &

共 19 条

[1]

BREW K, 1967, J BIOL CHEM, V242, P3747

[2] PURIFICATION AND SOME PROPERTIES OF BOVINE MILK LYSOZYME [J].