Identification, purification, and characterization of a secretory serine protease in an Indian strain of Leishmania donovani
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| Title |
Identification, purification, and characterization of a secretory
serine protease in an Indian strain of Leishmania donovani
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| Creator |
Choudhury, Rajdeep
Bhaumik, Siddhartha Kumar De, Tripti Chakraborti, Tapati |
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| Subject |
Infectious Diseases and Immunology
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| 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.
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| Publisher |
Kluwer
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| Date |
2009
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| 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. |
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| Relation |
http://dx.doi.org/10.1007/s11010-008-9849-7
http://www.eprints.iicb.res.in/232/ |
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