Source:http://linkedlifedata.com/resource/pubmed/id/15970451
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
2005-7-19
|
pubmed:abstractText |
A digestive beta-glucosidase cDNA was cloned from the silkworm, Bombyx mori. The B. mori beta-glucosidase cDNA contains an open reading frame of 1473 bp encoding 491 amino acid residues. The B. mori beta-glucosidase possesses the amino acid residues involved in catalysis and substrate binding conserved in glycosyl hydrolase family 1. Southern blot analysis of genomic DNA suggested the B. mori beta-glucosidase to be a single gene. Northern blot analysis of B. mori beta-glucosidase gene confirmed larval midgut-specific expression. The B. mori beta-glucosidase mRNA expression in larval midgut was detectable only during feeding period, whereas its expression was downregulated during starvation. The B. mori beta-glucosidase cDNA was expressed as a 57-kDa polypeptide in baculovirus-infected insect Sf9 cells, and the recombinant beta-glucosidase was active on cellobiose and lactose, but not active on salicin, indicating that the B. mori beta-glucosidase possesses the characteristics of the Class 2 enzyme. The enzyme activity of the purified recombinant beta-glucosidase expressed in baculovirus-infected insect cells was approximately 665 U per microg of recombinant B. mori beta-glucosidase. The purified recombinant B. mori beta-glucosidase showed the highest activity at 35 degrees C and pH 6.0, and were stable at 50 degrees C at least for 10 min. Treatment of recombinant virus-infected Sf9 cells with tunicamycin, a specific inhibitor of N-glycosylation, revealed that the recombinant B. mori beta-glucosidase is N-glycosylated, but the carbohydrate moieties are not essential for enzyme activity.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
1096-4959
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
141
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
418-27
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:15970451-Amino Acid Sequence,
pubmed-meshheading:15970451-Animals,
pubmed-meshheading:15970451-Bombyx,
pubmed-meshheading:15970451-Cloning, Molecular,
pubmed-meshheading:15970451-DNA, Complementary,
pubmed-meshheading:15970451-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:15970451-Gene Library,
pubmed-meshheading:15970451-Hydrogen-Ion Concentration,
pubmed-meshheading:15970451-Molecular Sequence Data,
pubmed-meshheading:15970451-Recombinant Proteins,
pubmed-meshheading:15970451-Sequence Homology, Amino Acid,
pubmed-meshheading:15970451-Species Specificity,
pubmed-meshheading:15970451-Temperature,
pubmed-meshheading:15970451-beta-Glucosidase
|
pubmed:year |
2005
|
pubmed:articleTitle |
A digestive beta-glucosidase from the silkworm, Bombyx mori: cDNA cloning, expression and enzymatic characterization.
|
pubmed:affiliation |
College of Natural Resources and Life Science, Dong-A University, Busan 604-714, Korea.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|