Studies on the Vibrio alginolyticus sucrose utilization system cloned into Escherichia coli
type: CreativeWork
description: This dissertation forms part of the study on the molecular biology of the aerobic, collagenolytic, halotolerant, gram-negative organism Vibrio alginolyticus. The cloning, expression and regulation of the v. alginolyticus sucrose utilization system in Escherichia coli is discussed and the results of a molecular analysis of the sucrase gene (scrA) are presented. The clone pVSlOO, containing a sucrose utilization system, was isolated from a genomic library of v. alginolyticus. Plasmid pVSlOO was mapped and the origin of its insert determined by Southern blotting and DNA hybridization. The number and sizes of the polypeptide products encoded by plasmid pVSlOO were determined by DNAdirected cell-free protein synthesis. The capsule, produced by transformed and untransformed E. coli JA221 cells, was shown to be independent of the presence of plasmid pVSlOO. The sucrase activity assay was optimized with respect to time, pH, temperature and salt requirements.
abstract: This dissertation forms part of the study on the molecular biology of the aerobic, collagenolytic, halotolerant, gram-negative organism Vibrio alginolyticus. The cloning, expression and regulation of the v. alginolyticus sucrose utilization system in Escherichia coli is discussed and the results of a molecular analysis of the sucrase gene (scrA) are presented. The clone pVSlOO, containing a sucrose utilization system, was isolated from a genomic library of v. alginolyticus. Plasmid pVSlOO was mapped and the origin of its insert determined by Southern blotting and DNA hybridization. The number and sizes of the polypeptide products encoded by plasmid pVSlOO were determined by DNAdirected cell-free protein synthesis. The capsule, produced by transformed and untransformed E. coli JA221 cells, was shown to be independent of the presence of plasmid pVSlOO. The sucrase activity assay was optimized with respect to time, pH, temperature and salt requirements.
author: Scholle, Renate Regina
language: eng
date published: 1989
date modified: 2026-07-22T22:22:50Z
provider: University of Cape Town
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: Department of Molecular and Cell Biology

PropertyValue
property ID: Handle
value: http://hdl.handle.net/11427/21906