Kinetics of Bacterial Phospholipase C Activity at Micellar Interfaces: Effect of Substrate Aggregate Microstructure and a Model for the Kinetic Parameters-Reference-Cited by-同舟云学术

Kinetics of Bacterial Phospholipase C Activity at Micellar Interfaces: Effect of Substrate Aggregate Microstructure and a Model for the Kinetic Parameters

Published:2008-12-03 Issue:51 Volume:112 Page:16741-16751
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Singh Jasmeet¹,Ranganathan Radha¹,Hajdu Joseph¹

Affiliation:

1. Department of Physics, Department of Chemistry and Biochemistry, and Center for Supramolecular Studies, California State University, Northridge, California 91330-8268

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp807067g

Reference46 articles.

1. Pancreatic porcine phospholipase A2 catalyzed hydrolysis of phosphatidylcholine in lecithin-bile salt mixed micelles: Kinetic studies in a lecithin-sodium cholate system

2. A Novel Class of Zinc-Binding Inhibitors for the Phosphatidylcholine-Preferring Phospholipase C from Bacillus cereus

3. Diversity of group types, regulation, and function of phospholipase A2.

4. The growing phospholipase A2 superfamily of signal transduction enzymes

5. Phospholipase A2in Eicosanoid Generation

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