ACETYLATED PECTIC ACID AS A SUBSTRATE OF VI-PHAGES DEACETYLASE

被引：1

作者：

KWIATKOWSKI, B

JASTRZEMSKI, KB

机构：

[1] Medical Academy, Institute of Medical Biology, Department of Physios and Biophysics, Debinki 1

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 91卷 / 03期

关键词：

D O I：

10.1016/0006-291X(79)91941-7

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 conditions of obtaining [14C] acetylated pectic acid with a high specific activity are presented. On the basis of radioisotope measurements of the liberated, labelled acetic acid, the activity of deacetylase associated with the ViI, ViII and ViIII phage particle was determined. It has been shown that acetylated pectic acid is a substrate for the enzyme of those phages. The conditions of identifying the deacetylase are presented; it has been shown that the activity of Vi phage II enzyme is repressed by the phosphate buffer. In a system analogous to the one used for the Vipolysaccharide, the receptor activity of the acetylated pectic acid can not be shown. © 1979.

引用

页码：730 / 738

页数：9

共 14 条

[1] ULTRASTRUCTURE OF VI PHAGES I TO VII OF SALMONELLA-TYPHI [J].