Further characterization of the acidic GPI-hydrolyzing phospholipase present in human sera.
Braz J Med Biol Res
; 27(2): 383-7, 1994 Feb.
Article
em En
| MEDLINE
| ID: mdl-8081253
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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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfolipase D
/
Glicoproteínas Variantes de Superfície de Trypanosoma
/
Glicosilfosfatidilinositóis
/
Lipase
Limite:
Humans
Idioma:
En
Revista:
Braz J Med Biol Res
Ano de publicação:
1994
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Brasil