Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

Maximizing plasmid stability and production of released proteins in Yersinia enterocolitica

Article Abstract:

A study of the roles of temperature, calcium and pH in the expression of the 25-kDa protein YopE and other Yops produced by Yersinia enterocolitica showed that the lowest temperature at which plasma-encoded proteins are expressed in quantity is 32 degrees Celsius, while the highest calcium concentration for their full expression was 445 to 545 micromoles. pYV stability is also found to be enhanced at low pH. Results provide new approaches for enhancing enrichment, isolation and identification of pathogenic YEP strains of Y. enterocolitica from natural or clinical sources.

Author: Bhaduri, Saumya, Li, Huaiyu, Magee, Wayne E.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Research, Plasmids, Yersinia enterocolitica

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Population genetics of human, animal, and environmental Yersinia strains

Article Abstract:

The possibility of epidemiologically correlating human, animal and environmental isolates was investigated. This involved the measurement of genetic relatednessand the analysis of genetic distances among and between strains of nine Yersinia species. Bacterial isolates were subjected to phenotypic characterization, genetic analysis and statistical analysis. The different Yersinia species exhibited variable genetic distances which shows different levels of DNA homlogy among the species.

Author: Peduzzi, Raffaele, Dolina, Marisa
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1993
Genetic aspects, Yersinia

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


A surface-focused biotinylation procedure identifies the Yersinia pestis catalase KatY as a membrane-associated but non-surface-located protein

Article Abstract:

The major surface proteins of the plaque bacterium Yersinia pestis which was identified by applying a novel surface biotinylation method followed by NeutrAvidin (NA) bead capture is presented.

Author: Borchers, Christoph H., Myers-Morales, Tanya, Cowan, Clarissa, Gray, Michael E., Wulff, Christine R., Parker, Carol E., Straley, Susan C.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2007
Analysis, Physiological aspects, Growth, Membrane proteins, Liquid chromatography, Company growth, Structure, Yersinia pestis, Biotin

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA

Similar abstracts:
  • Abstracts: Molecular cloning and duplication of the nematode sex-determining gene tra-1
  • Abstracts: Activity, expression and function of a second Drosophila protein kinase A catalytic subunit gene. The embryonically active gene, unkempt, of Drosophila encodes a Cys(sub 3)His finger protein
  • Abstracts: Mechanism of action of regulatory proteins encoded by complex retroviruses. part 2 The Rhizobium-plant symbiosis
  • Abstracts: Biotic and abiotic factors affecting plasmid transfer in Escherichia coli. Nitroaromatics are substrates for the TOL plasmid upper-pathway enzymes
  • Abstracts: Production of extracellular proteins by the biocontrol fungus Gliocladium virens. Partial purification and characterization of manganese-oxidizing factors of Pseudomonas fluorescens GB-1
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2025 Advameg, Inc.