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

Content Provider	Springer Nature Link
Author	Choudhury, Rajdeep Bhaumik, Siddhartha Kumar De, Tripti Chakraborti, Tapati
Copyright Year	2008
Abstract	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-α-p-tosyl-l-arginine methylester (TAME) appeared to be relatively better substrate among the commonly used synthetic substrates. The enzyme was inhibited by Ca$^{2+}$ and Mn$^{2+}$, but activated by Zn$^{2+}$. The protease could play important role(s) in the pathogenesis of visceral leishmaniasis or kala-azar.
Starting Page	1
Ending Page	14
Page Count	14
File Format	PDF
ISSN	03008177
Journal	Molecular and Cellular Biochemistry
Volume Number	320
Issue Number	1-2
e-ISSN	15734919
Language	English
Publisher	Springer US
Publisher Date	2008-06-29
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Leishmania donovani (MHOM/IN/1983/AG83) Aprotinin Extracellular serine protease Extracellular matrix proteins Cardiology Oncology Medical Biochemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Clinical Biochemistry Molecular Biology

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