rdf:type |
|
lifeskim:mentions |
umls-concept:C0006556,
umls-concept:C0009015,
umls-concept:C0014834,
umls-concept:C0017262,
umls-concept:C0057489,
umls-concept:C0185117,
umls-concept:C0323677,
umls-concept:C0679058,
umls-concept:C1511780,
umls-concept:C1547699,
umls-concept:C2700640,
umls-concept:C2717971,
umls-concept:C2911684
|
pubmed:issue |
1
|
pubmed:dateCreated |
1996-2-9
|
pubmed:databankReference |
|
pubmed:abstractText |
Der f 3 is one of the allergens produced by house dust mite Dermatophagoides farinae showing serine protease activity. Based on its amino acid sequence, a cDNA clone encoding Der f 3 was isolated from a cDNA library of D. farinae. Sequencing analysis of the clone revealed the presence of an open reading frame of 780 bp, which encodes a mature protein of 232 amino acids with 27 amino acids of pre-pro sequence at the N-terminus. When proDer f 3 was produced in Escherichia coli as a fused protein with glutathione-S-transferase, the fused protein was accumulated as inclusion bodies. The protein purified with 8 M urea and glutathione-affinity column chromatography, however, did not show protease activity. When an arginine residue was introduced at the C-terminus of the pro-region in place of threonine, removal of the pro-region to produce an active mature protease was observed. The specificity and the activity of this recombinant protease were almost the same as those of native Der f 3.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
11
|
pubmed:volume |
377
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
62-6
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:8543021-Allergens,
pubmed-meshheading:8543021-Amino Acid Sequence,
pubmed-meshheading:8543021-Antigens, Dermatophagoides,
pubmed-meshheading:8543021-Base Sequence,
pubmed-meshheading:8543021-Chromatography, Affinity,
pubmed-meshheading:8543021-Cloning, Molecular,
pubmed-meshheading:8543021-DNA, Complementary,
pubmed-meshheading:8543021-Escherichia coli,
pubmed-meshheading:8543021-Gene Expression,
pubmed-meshheading:8543021-Glutathione Transferase,
pubmed-meshheading:8543021-Glycoproteins,
pubmed-meshheading:8543021-Humans,
pubmed-meshheading:8543021-Immunoglobulin E,
pubmed-meshheading:8543021-Molecular Sequence Data,
pubmed-meshheading:8543021-Recombinant Fusion Proteins,
pubmed-meshheading:8543021-Serine Endopeptidases
|
pubmed:year |
1995
|
pubmed:articleTitle |
Cloning and expression in Escherichia coli of cDNA encoding house dust mite allergen Der f 3, serine protease from Dermatophagoides farinae.
|
pubmed:affiliation |
Central Research Laboratories, Asahi Breweries, Ltd., Tokyo, Japan.
|
pubmed:publicationType |
Journal Article
|