Substrate specificities and properties of human phospholipases A2 in a mixed vesicle model.

Structural and enzymological properties of cellular phospholipases A2.

Differential interfacial and substrate binding modes of mammalian pancreatic phospholipases A2: a comparison among human, bovine, and porcine enzymes.

To identify the residues essential for interfacial binding and substrate binding of human pancreatic phospholipase A2 (hpPLA2), several ionic residues in the putative interfacial binding surface (R6E, K7E, K10E, and K116E) and substrate binding site (D53K and K56E) were mutated. Interfacial affinity of these mutants was measured using anionic polymerized liposomes, and their enzymatic activity ...

Secretory phospholipases A2 activate selective functions in human eosinophils.

Secretory phospholipases A(2) (sPLA(2)s) are released in large amounts in the blood of patients with systemic inflammatory diseases and accumulate at sites of chronic inflammation, such as the airways of patients with bronchial asthma. Blood eosinophils or eosinophils recruited in inflammatory areas therefore can be exposed in vivo to high concentrations of sPLA(2). We have examined the effects...

Comparison of the properties of human group II phospholipase A2 with other secretory phospholipases.

The human group II secretory phospholipase A, (sPLA,) has been implicated in a number of inflammatory conditions, including rheumatoid arthritis. A continuous fluorescence displacement assay which measures the release of long chain fatty acids [l] has been used to investigate the activity of a recombinant form of this human enzyme (HR PLAJ and is reported here for the first time. Secretory phos...

Phosphoprotein Phosphatase of Soybean Hypocotyls: PURIFICATION, PROPERTIES, AND SUBSTRATE SPECIFICITIES .

A soybean histone-type protein kinase was used to prepare (32)P-labeled histone H1 as substrate for purification and characterization of a phosphoprotein phosphatase (EC 3.1.3.16) from soybean hypocotyls. The phosphatase has been purified 169-fold by ammonium sulfate fractionation, ethanol precipitation, and chromatography on Sephadex G-150, DEAE-Sephadex A-25 and Sephadex G-100. The activity o...