Further characterization of the acidic GPI-hydrolyzing phospholipase present in human sera
Braz. j. med. biol. res
;
27(2): 383-7, Feb. 1994. ilus
Article
in English
| LILACS
| ID: lil-140279
RESUMO
A phospholipase from human serum capable of hydrolyzing glycosylphosphatidylinositol membrane anchors was described and partially characterized by our group some years ago. This activity presented a pH optimum between 5.0 and 6.0 and was inhibited by EDTA, EGTA and 1,10-phenanthroline. Partial purification showed that the enzyme was a glycoprotein with an apparent molecular weight of 140 kDa as judged by gel filtration. Other investigators characterized at the same time a phospholipase D with similar properties but with a pH optimum near 7.5. We now confirm that the human serum enzyme is indeed a phospholipase D capable of hydrolyzing mfVSG and glycolipids A and C from T. brucei. Isoelectric focusing of whole sera suggests the presence of two isoforms, one with a pI of 4.7 which was the form previously purified by our group, and others with pI from 6.2 to 7.4
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Index:
LILACS (Americas)
Main subject:
Phosphatidylinositols
/
Phospholipase D
/
Plasma
/
Glycolipids
/
Hydrolysis
Limits:
Humans
Language:
English
Journal:
Braz. j. med. biol. res
Journal subject:
Biology
/
Medicine
Year:
1994
Type:
Article
/
Congress and conference
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