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http://repository.kln.ac.lk/handle/123456789/3777
Title: | Arginine Decarboxylase from the pathogenic fungi, Colleotrichum gleosporosides : Purification and Properties |
Authors: | Weerasooriya, M.K.B. Handagiripathira, H.M.N.L. Wijewickrama, G.T. |
Keywords: | Anthracnose; Colletotrichum gleosporoides; Arginine decarboxylase; polyamine metabolism |
Issue Date: | 2003 |
Publisher: | Journal of Science of the University of Kelaniya Sri Lanka |
Citation: | Weerasooriya, M.K.B., Handagiripathira, H.M.N.L. and Wijewickrama, G.T. 2003. Arginine Decarboxylase from the pathogenic fungi, Colleotrichum gleosporosides: Purification and Properties. Journal of Science of the University of Kelaniya, 01: 23-33. |
Abstract: | Arginine decarboxylase, a polyamine biosynthetic enzyme, was isolated from a phytopathogenic fungi, Colletotrichum gleosporoides, which causes Anthracnose in wide range of plants in many parts ofthe world. The enzyme was purified 25 fold with 16.7% recovery by elution through Sepharose 4B gel column and DEAE Cellulose ion exchange column. As determined by Sepharose 4B gel chromatography, the native molecular mass of the purified enzyme was ~265kDa. SDS-PAGE of the purified enzyme showed two bands around 65 kDa and ~25 kDa, suggesting that possibly this enzyme could be a hexamer of above two sub units. Optimum pH and temperature for the enzyme was 5.2 and 40�C respectively . Beyond 50�C enzyme activity slowly declined and was almost deactivated by 80�C. Approximate Km of the enzyme for the substrate arginine was 67mM. |
URI: | http://repository.kln.ac.lk/handle/123456789/3777 |
ISSN: | ISSN 1391-9210 |
Appears in Collections: | Volume 01 - 2003 |
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