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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1993-7-15
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pubmed:abstractText |
A method for immobilizing barley oxalate oxidase to zirconia coated alkylamine glass through the process of glutaraldehyde coupling has been described. The immobilized enzyme retained 97.2% of the specific activity, with a conjugation yield of 6.63 mg/g support and showed an increase in optimum pH. The Km value of immobilized enzyme was unaltered but Vmax was decreased compared to free enzyme. The conjugated enzyme was stable at 4 degrees C for 2 years. A number of inorganic ions and metabolic substances did not denature the immobilized enzyme. The clinical importance of this work is demonstrated.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0301-1208
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
54-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
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pubmed:year |
1993
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pubmed:articleTitle |
Barley oxalate oxidase immobilized on zirconia-coated alkylamine glass using glutaraldehyde.
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pubmed:affiliation |
Department of Bio-Sciences, Maharshi Dayanand University, Rohtak, India.
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pubmed:publicationType |
Journal Article
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