These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Partial purification and some properties of a phospholipase C from Pseudomonas sp. strain KS3.2.
    Author: Sugimori D, Nakamura M.
    Journal: Biosci Biotechnol Biochem; 2006 Feb; 70(2):535-7. PubMed ID: 16495676.
    Abstract:
    An extracellular phospholipase C was partially purified from Pseudomonas sp. strain KS3.2. The enzyme was composed of an approximately 18-kDa peptide. Maximal enzyme activity was found at pH 7.2 and 50 degrees C. The enzyme retained activity between pH 8 and 9, and 50% activity at about 52 degrees C for 30 min. The enzyme sample showed the highest activity on phosphatidylcholine and low activity toward other phospholipids.
    [Abstract] [Full Text] [Related] [New Search]