Proteinases of Leishmania mexicana amastigotes and promastigotes: Analysis by gel electrophoresis |
| |
Authors: | Michael J. North Graham H. Coombs |
| |
Affiliation: | 1. Department of Biochemistry, University of Stirling, Stirling, FK9 4LA, Scotland;2. Department of Zoology, University of Glasgow, Glasgow, G12 8QQ, Scotland |
| |
Abstract: | The proteinases of Leishmania mexicana mexicana amastigotes and promastigotes have been analysed by electrophoresis on polyacrylamide gels containing denatured haemoglobin. Eleven bands of activity were detected indicating multiple proteinases. There were significant quantitative and qualitative differences between the proteinases of the two developmental forms. Four, B–E, were present in both forms but were of much higher activity in the amastigote. There were two major activities in promastigotes, A and D. The other proteinases, F–K, were of lower activity; I and K were not detected in promastigotes. All proteinases were active optimally at pH 4.0. Most of them, including the major proteinases A–E, were thiol proteinases since they were stimulated by 1 mM dithiothreitol and were sensitive to inhibitors such as HgCl2, leupeptin, antipain and iodoacetic acid. |
| |
Keywords: | Proteinases Gel electrophoresis DAN diazoacetyl-DL-norleucine methyl ester DTT dithiothreitol FCS foetal calf serum TLCK TPCK 1-chloro-4-phenyl-3-tosylamido-L-butane-2-one PMSF phenylmethylsulphonyl fluoride |
本文献已被 ScienceDirect 等数据库收录! |
|