THE LYTIC ENZYME OF THE PSEUDOMONAS PHAGE PHI-6 - PURIFICATION AND BIOCHEMICAL-CHARACTERIZATION

被引：50

作者：

CALDENTEY, J

BAMFORD, DH

机构：

[1] Department of Genetics, University of Helsinki, Helsinki

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1159卷 / 01期

基金：

芬兰科学院;

关键词：

BACTERIOPHAGE; LYTIC ENZYME; PROTEIN PURIFICATION; ENZYMATIC ACTIVITY;

D O I：

10.1016/0167-4838(92)90073-M

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：

The lytic enzyme of the lipid-containing bacteriophage phi6, protein P5, has been purified to apparent homogeneity from disrupted viral particles. The enzyme is a monomer with a molecular mass of approx. 24 kDa. The optimal pH for P5 activity is 8.5 and the protein is readily inactivated at temperatures above 20-degrees-C. Protein P5 is active against several Gram-negative bacteria, but no activity against Gram-positive species was detected. Analysis of cell wall digests indicates that P5 is not a glycosidase, but an endopeptidase splitting the peptide bridge formed by meso-diaminopimelic acid and D-alanine.

引用

页码：44 / 50

页数：7

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