Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/3513
Title: Purification and partial characterization of α-D-mannosidase from Erythrina indica seeds
Authors: Kestwal, Rakesh M
Bhide, Shobhana V
Keywords: Erythrina indica
⍺-D-mannosidase
Purification
con-A CL seralose
Zinc
Issue Date: Jun-2005
Publisher: CSIR
Series/Report no.: A 23 J 1/14, C 07 K
Abstract: ⍺-D-Mannosidase (EC: 3.2.1.24), a glycoprotein with 8.6% carbohydrate was purified (26 fold purification) to homogeneity from Erythrina indica seeds, by gel filtration on Bio-Gel P-100 and affinity chromatography on Con-A CL Seralose. The enzyme had the molecular mass of 124 kDa and 127 kDa by gel filtration and SDS-PAGE, respectively. The optimum pH and temperature for enzyme activity were found to be 4.6 and 50ºC, respectively. The Km value for the enzyme was 2.1 mM for p-nitrophenyl-α-D-mannopyranoside. The enzyme activity was found to depend on the presence of Zn²⁺. Chemical modification studies revealed the involvement of tryptophan, serine and cysteine for enzyme activity.
Description: 156-160
URI: http://hdl.handle.net/123456789/3513
ISSN: 0301-1208
Appears in Collections:IJBB Vol.42(3) [June 2005]

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