Title : Purification and characterization of PLC-beta m, a muscarinic cholinergic regulated phospholipase C from rabbit brain membrane.

Pub. Date : 1990 Aug 13

PMID : 2166589






6 Functional Relationships(s)
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Protein Name
Organism
1 Two isozymes of phosphoinositide-specific phospholipase C were isolated and purified from salt-washed rabbit brain membranes. Salts LOC100009319 Oryctolagus cuniculus
2 Sodium pyrophosphate and sodium fluoride stimulated phospholipase C activity of both isozymes. sodium pyrophosphate LOC100009319 Oryctolagus cuniculus
3 Sodium pyrophosphate and sodium fluoride stimulated phospholipase C activity of both isozymes. Sodium Fluoride LOC100009319 Oryctolagus cuniculus
4 Polyclonal antibodies raised against PLC-beta m were able to inhibit carbachol and GTP gamma S stimulated phospholipase C activity in 2 M KCl washed rabbit cortical membranes. Guanosine Triphosphate LOC100009319 Oryctolagus cuniculus
5 Polyclonal antibodies raised against PLC-beta m were able to inhibit carbachol and GTP gamma S stimulated phospholipase C activity in 2 M KCl washed rabbit cortical membranes. Sulfur LOC100009319 Oryctolagus cuniculus
6 Polyclonal antibodies raised against PLC-beta m were able to inhibit carbachol and GTP gamma S stimulated phospholipase C activity in 2 M KCl washed rabbit cortical membranes. Potassium Chloride LOC100009319 Oryctolagus cuniculus