Record Details

Identification, purification, and characterization of a secretory serine protease in an Indian strain of Leishmania donovani

EPrints@IICB

View Archive Info
 
 
Field Value
 
Title Identification, purification, and characterization of a secretory
serine protease in an Indian strain of Leishmania donovani
 
Creator Choudhury, Rajdeep
Bhaumik, Siddhartha Kumar
De, Tripti
Chakraborti, Tapati
 
Subject Infectious Diseases and Immunology
 
Description An aprotinin sensitive serine protease was
identified in the culture supernatant of the Indian strain of
Leishmania donovani (MHOM/IN/1983/AG83). The protease
was subsequently purified and characterized. The
apparent molecular mass of the enzyme was 115 kDa in
SDS-PAGE under non-reducing condition, while on
reduction it showed a 56 kDa protein band indicating that
the protease is a dimeric protein. The purified enzyme was
optimally active at the pH and temperature of 7.5 and
28�C, respectively. Assays of thermal stability indicated
that the enzyme preserved 59% of activity even after pretreatment
at 42�C for 1 h. The purified protease was not
glycosylated and its isoelectric pI was 5.0. N-a-p-tosyl-Larginine
methylester (TAME) appeared to be relatively
better substrate among the commonly used synthetic substrates.
The enzyme was inhibited by Ca2? and Mn2?, but
activated by Zn2?. The protease could play important
role(s) in the pathogenesis of visceral leishmaniasis or
kala-azar.
 
Publisher Kluwer
 
Date 2009
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/232/1/MOLECULAR_AND_CELLULAR_BIOCHEMISTRY%2C320%2C(1%2D2)%2C1%2D14%2C2009[129].pdf
Choudhury, Rajdeep and Bhaumik, Siddhartha Kumar and De, Tripti and Chakraborti, Tapati (2009) Identification, purification, and characterization of a secretory serine protease in an Indian strain of Leishmania donovani. Molecular and Cellular Biochemistry, 320 (1-2). 01-14.
 
Relation http://dx.doi.org/10.1007/s11010-008-9849-7
http://www.eprints.iicb.res.in/232/