Cell-Associated and Extracellular Proteinases in Blastocrithidia culicis: Influence of Growth Conditions |
| |
Authors: | André Luis Souza dos Santos Celina Monteiro Abreu Letícia Moulin Batista Celuta Sales Alviano Rosangela Maria de Araújo Soares |
| |
Institution: | Departamento de Microbiologia Geral, Instituto de Microbiologia Professor Paulo de Góes (IMPPG), Centro de Ciências da Saúde (CCS), Bloco I, Universidade Federal do Rio de Janeiro (UFRJ), Ilha do Fund?o, 21941-590, Rio de Janeiro, RJ, Brazil, BR
|
| |
Abstract: | The proteinase profile of Blastocrithidia culicis was analyzed, as well as how different growth conditions influenced its expression by gelatin-SDS-PAGE and the use of specific
proteinase inhibitors. Multiple cell-associated proteinases with molecular masses corresponding to 33, 55, 60 kDa (cysteine
proteinases) and 77, 80, 90, and 108 kDa (metalloproteinases) were detected using these methods. All the metalloproteinases
identified were partitioned into the detergent phase after Triton X-114 extract, suggesting that they are membrane-bound,
while all cysteine proteinases were partitioned into the aqueous phase. The proteolytic zymograms were similar when three
different media were used for variable times of incubation. However, few quantitative and qualitative changes were observed.
The secreted proteinase profile showed an heterogeneous pattern of enzymatic activities whose expression was dependent on
time of growth and medium composition. However, the extracellular proteinase activities were abolished by 1,10-phenanthroline,
suggesting that all of them are zinc-metalloproteinases.
Received: 25 October 2000 / Accepted: 10 January 2001 |
| |
Keywords: | |
本文献已被 PubMed SpringerLink 等数据库收录! |
|