Crithidia guilhermei: gelatin- and haemoglobin-degrading extracellular metalloproteinases.

Abstract:

:The extracellular metalloproteinases of the insect trypanosomatid Crithidia guilhermei were characterized through the incorporation of different protein substrates (gelatin, casein, haemoglobin, and bovine serum albumin) into SDS-PAGE. Two gelatinases (60 and 80 kDa) showed ability to degrade casein as well and a 67-kDa enzyme presented the broadest specificity since it was also able to degrade casein and haemoglobin. Besides the 67-kDa extracellular proteinases detected on haemoglobin-SDS-PAGE, a 43-kDa haemoglobinase was only observed with this substrate. All C. guilhermei proteinases were incapable of using bovine serum albumin. C. guilhermei was also grown in four different culture media and the best proteinase production was reached using yeast extract-peptone medium containing glucose as the major carbon source. The results point to the importance of the use of distinct culture media and proteinaceous substrates on the characterization of extracellular proteolytic activities in trypanosomatids, since alterations in growth conditions and methods of detection could lead to distinct proteolytic profiles.

journal_name

Exp Parasitol

authors

de Melo AC,d'Avila-Levy CM,Branquinha MH,Vermelho AB

doi

10.1016/s0014-4894(03)00037-7

keywords:

subject

Has Abstract

pub_date

2002-11-01 00:00:00

pages

150-6

issue

3-4

eissn

0014-4894

issn

1090-2449

journal_volume

102

pub_type

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