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The lysosomal gp63‐related protein in Leishmania mexicana amastigotes is a soluble metalloproteinase with an acidic pH optimum
Author(s) -
Ilg Thomas,
Harbecke Dorothee,
Overath Peter
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81049-6
Subject(s) - amastigote , leishmania mexicana , metalloproteinase , chemistry , biochemistry , leishmania , enzyme , parasite hosting , world wide web , computer science
Leishmania mexicana amastigotes express a lysosomal protein, which is antigenically related to the promastigote surface metalloproteinase (gp63). It is shown that the purified gp63‐related protein from amastigote is also an active metalloproteinase. The pH‐optimum of the enzyme is acidic, similar to lysosomal cysteine proteinases, but distinct from the neutral to basic pH‐optimum of the promastigote surface proteinase. This study appears to be the first report on a metalloproteinase with a lysosomal localization.