Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

Development of a genetic transformation system for an alga-lysing bacterium

Article Abstract:

Alteromonas sp. strain A28 that was determined from a coastal seawater lysed a number of algae. The alga-lytic bacteria was prepared using the soft-agar overlayer method while plasmid extractions were carried out by the alkalin lysis technique. Alteromonas cells were determined by electroporation after cells were grown overnight. The efficiency of the chimeric plasmid transformation of A28 was dependent with the source of plasmid DNA.

Author: Kato, Junichi, Kuroda, Akio, Mitsutani, Atsushi, Ohtake, Hisao, Amie, Junya, Murata, Yoshinori
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Algae, Genetic aspects, Water bloom, Algal blooms

User Contributions:

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

CAPTCHA


Inhibition of quorum sensing in Pseudomonas aeruginosa by N-acyl cyclopentylamides

Article Abstract:

The ability of a series of structural analogs of C8-cyclopentylamide (CPA) to inhibit quorum sensing in Pseudomonas aeruginosa (PAO) is examined. N-decanoyl cyclopentylamide (C10-CPA) was found to be the strongest quorum-sensing inhibitor that interferes with expression of Pseudomonas aeruginosa virulence factors regulated by the las and rhl quorum-sensing systems.

Author: Kato, Junichi, Takiguchi, Noboru, Kuroda, Akio, Ikeda, Tsukasa, Ohtake, Hisao, Ishida, Takenori
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2007
Science & research, Research, Analysis, Polymerase chain reaction, Genetic transcription, Transcription (Genetics), Pseudomonas aeruginosa, Quorum sensing

User Contributions:

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

CAPTCHA


Involvement of an extracellular protease in algicidal activity of the marine bacterium Pseudoalteromonas sp strain A28

Article Abstract:

Research reveal that extracellular product of the marine bacterium Pseudoalteromonas sp strain A28 possesses algicidal activity mediated by protease. Studies with the purified enzyme and protease minus mutants show that extracellularly produced serine protease is responsible for the algicidal activity against the diatom.

Author: Lee, Sun-Og, Kato, Junichi, Takiguchi, Noboru, Kuroda, Akio, Ikeda, Tsukasa, Mitsutani, Atsushi, Ohtake, Hisao
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000
United States, Japan, Statistical Data Included, Cell death, Proteases, Marine bacteria, Diatoms

User Contributions:

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

CAPTCHA


Subjects list: Physiological aspects
Similar abstracts:
  • Abstracts: Development of a fluorogenic 5' nuclease PCR assay for detection of the ail gene of pathogenic yersinia enterocolitica
  • Abstracts: Suppression of Ras-stimulated transformation by the JNK signal transduction pathway. Signal transduction by the JNK group of MAP kinases
  • Abstracts: Selective coactivation of estrogen-dependent transcription by CITED1 CBP/p300-binding protein. Yeast heterochromatin is a dynamic structure that requires silencers continuously
  • Abstracts: Isolation and characterization of a novel toluene-degrading, sulfate-reducing bacterium. Desulfotomaculum and methanobacterium spp. dominate a 4- to 5-kilometer-deep fault
  • Abstracts: Heterologous production of antimicrobial peptides in Propionibacterium freudenreichii. Biochemical and genetic characterization of propionicin T1, a new bacteriocin from Propionibacterium thoenii
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.