FURTHER CHARACTERIZATION OF THE ACIDIC GPI-HYDROLYZING PHOSPHOLIPASE PRESENT IN HUMAN SERA

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Data
1994-02-01
Autores
Stambuk, Boris Juan Carlos Ugarte [UNIFESP]
Cardosodealmeida, M. L.
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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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Brazilian Journal Of Medical And Biological Research. Sao Paulo: Assoc Bras Divulg Cientifica, v. 27, n. 2, p. 383-387, 1994.
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