Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.5 (neuropathy target esterase)
1,070 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phospholipase B (EC 3.1.1.5) which hydrolyzes phospholipids in the alpha and beta positions was demonstrated in murine leukocytes using light and electron microscopic histochemical techniques. Leukocytes (neutrophils, lymphocytes, macrophages, eosinophils) were harvested from peritoneal exudates of mice. Cells were fixed in 4% calcium-formol fixative for 10 min at 4 degrees C for light microscopy and 30 min at room temperature for electron microscopy, after which they were incubated at 37 degrees C in medium at pH 6.6 containing 2 microM lysolecithin and CaCl2. The fatty acids released during the hydrolytic reaction were trapped as a calcium precipitate and were converted to a cobalt precipitate for light microscopy by treatment with cobalt acetate or to a lead precipitate for electron microscopy by treatment with lead nitrate. The reaction products were observed to be present in eosinophils and absent in neutrophils, lymphocytes and macrophages. It is concluded that the eosinophilic leukocyte is the carrier cell for phospholipase B in inflammatory reactions.
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PMID:Light and electron microscopic demonstration of phospholipase B activity in the mouse eosinophil. 334 75

A method has been developed for electron microscopic histochemical demonstration of phospholipase B, (lecithinase B, E C 3.1.1.5, lysolecithin acyl hydrolase), which hydrolyzes alpha- and beta-positions of phospholipids in mouse liver, kidney and adrenal tissues. Tissues either fixed in cold 1% paraformaldehyde or unfixed were cut into 40 micrometers frozen sections and were incubated at 37 degrees C in a medium at pH 6.6 or 4.5 containing 2 microM lysolecithin and 0.25 mM CaCl2 for 20 min. The fatty acids liberated by enzymatic hydrolysis were trapped as calcium precipitate and were converted to lead precipitate by treatment with lead nitrate. The reaction products were observed by electron microscopy to be localized on the end of the smooth endoplasmic reticulum at pH 6.6 and in lysosomes and lipid droplets at pH 4.5. It is concluded that the products showed the localization of phospholipase B activity.
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PMID:Electron microscopic demonstration of phospholipase B activity in the liver and the kidney of the mouse. 671 5