Interfacial kinetic and binding properties of mammalian group IVB phospholipase A2 (cPLA2β) and comparison with the other cPLA2 isoforms

Journal of Biological Chemistry

Volumn 285, Issue 46, 2010, Pages 36100-36111

  Ghomashchi, Farideh ^a   Naika, Gajendra S ^a   Bollinger, James G ^a   Aloulou, Ahmed ^a   Lehr, Matthias ^b   Leslie, Christina C ^c   Gelb, Michael H ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b UNIVERSITY OF MÜNSTER   (Germany)

^c DEPARTMENT OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION PATTERNS; ANIONIC PHOSPHOLIPIDS; BINDING PROPERTIES; BINDING SURFACE; CARDIOLIPINS; CYTOSOLIC; IN-VITRO; INTERFACIAL BINDING; INTERFACIAL KINETIC; ISOFORMS; PHOSPHATIDYLCHOLINE; PHOSPHOINOSITIDES; PHOSPHOLIPASE A; RECOMBINANT PROTEIN; SELECTIVE INHIBITORS;

ANTIGENS; BINDING ENERGY; CALCIUM; MAMMALS; PROTEINS;

PHOSPHOLIPIDS;

CALCIUM ION; CARDIOLIPIN; ISOENZYME; LYSOPHOSPHOLIPASE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLINOSITIDE; PHOSPHOLIPASE A1; PHOSPHOLIPASE A2; PHOSPHOLIPASE A2 ALPHA; PHOSPHOLIPASE A2 BETA; PHOSPHOLIPASE A2 DELTA; PHOSPHOLIPASE A2 EPSILON; PHOSPHOLIPASE A2 GAMMA; PHOSPHOLIPASE A2 GROUP IV; PHOSPHOLIPASE A2 INHIBITOR; PHOSPHOLIPASE A2 ZETA; PHOSPHOLIPID; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CALCIUM BINDING; CELL VACUOLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME REGULATION; IN VITRO STUDY; MAMMAL; PRIORITY JOURNAL; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; BINDING SITES; BIOCATALYSIS; CALCIUM; CELL LINE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME INHIBITORS; GROUP IV PHOSPHOLIPASES A2; HUMANS; HYDROLYSIS; ISOENZYMES; KINETICS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTATION; PHOSPHOLIPASES A2, CYTOSOLIC; PHOSPHOLIPIDS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SPODOPTERA;

MAMMALIA;

EID: 78149268304     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.165647     Document Type: Article

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