Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

Purification and structural determination of an inhibitor of Starfish oocyte maturation from a Bacillus species

Article Abstract:

An oocyst maturation inhibiting substance (OMIS) obtained from a bacterial culture has been found to inhibit the 1-methyladenine-induced oocyte maturation but not the dithiothreitol-induced maturation. The OMIS is the lactone of 3-hydroxy-13-methyltetradecanoyl-Glu-Leu-Leu-Val-Asp-Leu-Leu. Though the amino acid configurations have not been determined, the structure and inhibition activity of this OMIS are the same as that of surfactin. OMIS inhibits the oocyte maturation by affecting either the hormone signal transduction or the cell cycle regulation.

Author: Toraya, Tetsuo, Maoka, Takuya, Tsuji, Hiroki, Kobayashi, Motoyuki
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
Oocytes, Oocyte donation, Animal development, Starfishes

User Contributions:

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

CAPTCHA


Purification and properties of ArfI, an alpha-L-arabinofuranosidase from Cytophaga xylanolytica

Article Abstract:

A study was conducted to determine purification and properties of alpha-L-arabinofuranosidase from Cytophaga xylanolytica. Purification was undertaken via anion exchange and hydrophobic interaction column chromatography. Results revealed that ArfI demonstrated zero hydrolytic activity toward a range of p-nitrophenyl- or 4-methylumbelliferyl-glycosides apart from arabinoside. Furthermore, ArfI was generally cytoplasmic which connotes that its activity in vivo is most suitable to hydrolysis of arabinose-containing oligosaccharides.

Author: Breznak, John A., Renner, Michael J.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Composition, Enzyme kinetics, Anaerobic bacteria, Furans, Vidarabine

User Contributions:

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

CAPTCHA


Production, purification, and characterization of a highly glucose-tolerant novel beta-glucosidase from Candida peltata

Article Abstract:

The beta-glucosidase produced and purified from Candida peltata hydrolyzes cellobiose, shows a synergistic interaction with cellulase and has high glucose tolerance. The enzyme is a monomeric protein with a molecular weight of 43,000, and has maximum activity at 50 degrees celsius and 5.0 pH. The beta-glucosidase has little transglucosylation activity. Divalent cations are unessential for the enzymatic activity which is unaffected by p-chloromercuribenzoate.

Author: Saha, Badal C., Bothast, Rodney J.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
Glucosidases, Alpha glucosidases, Candida

User Contributions:

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

CAPTCHA


Subjects list: Research
Similar abstracts:
  • Abstracts: Purification and characterization of a prolidase from Lactobacillus casei subsp. casei IFPL 731. Growth inhibition of metronidazole-susceptible and metronidazole-resistant strains of Gardnerella vaginalis by lactobacili in vitro
  • Abstracts: Purification and characterization of two xylanases from alkalophilic Cephalosporium sp. strain RYM-202. Glycine betaine: reserve form of choline in Penicillium fellutanum in low-sulfate medium
  • Abstracts: Evaluation of bottlenecks in the late stages of protein secretion in Bacillus subtilis. Direct selection of cloned DNA in Bacillus subtilis based on sucrose-induced lethality
  • Abstracts: Phylogenetic identification and in situ detection of individual microbial cells without cultivation. Microbial reductive dehalogenation
  • Abstracts: Antimycoplasma properties and application in cell culture of surfactin, a lipopeptide antibiotic from Bacillus subtilis
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.