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Purification and partial characterization of α-D-mannosidase from Erythrina indica seeds
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View Archive Info| Field | Value | |
| Title |
Purification and partial characterization of α-D-mannosidase from Erythrina indica seeds
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| Creator |
Kestwal, Rakesh M
Bhide, Shobhana V |
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| Subject |
Erythrina indica
⍺-D-mannosidase Purification con-A CL seralose Zinc |
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| Description |
156-160
⍺-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. |
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| Date |
2009-03-30T07:40:45Z
2009-03-30T07:40:45Z 2005-06 |
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| Type |
Article
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| Identifier |
0301-1208
http://hdl.handle.net/123456789/3513 |
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| Language |
en_US
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| Relation |
A 23 J 1/14, C 07 K
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| Publisher |
CSIR
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| Source |
IJBB Vol.42(3) [June 2005]
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