CLONING AND CHARACTERIZATION OF A MAJOR ALLERGEN OF THE HOUSE-DUST MITE, DERMATOPHAGOIDES-PTERONYSSINUS, HOMOLOGOUS WITH GLUTATHIONE-S-TRANSFERASE

被引：69
|
作者：
ONEILL, GM
DONOVAN, GR
BALDO, BA
机构：
[1] ROYAL N SHORE HOSP,KOLLING INST MED RES,ST LEONARDS,NSW 2065,AUSTRALIA
[2] UNIV SYDNEY,DEPT MED,SYDNEY,NSW,AUSTRALIA
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 1994年 / 1219卷 / 02期
基金：
英国医学研究理事会;
关键词：
GLUTATHIONE S-TRANSFERASE; IGE ANTIBODY; ALLERGY; (DERMATOPHAGOIDES-PTERONYSSINUS);
D O I：
10.1016/0167-4781(94)90080-9
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A major allergen of the house dust mite, Dermatophagoides pteronyssinus, has been identified and characterized from a lambda gt11 cDNA library of the mite. IgE antibodies from the sera of allergic patients that recognise the cloned polypeptide bind to an similar to 26 kDa polypeptide on a Western blot of reduced mite polypeptides. Nucleotide sequencing of the clone revealed a 219 amino acid open reading frame-encoding a protein with a derived molecular mass of 25589 Da and a pi of 6.3. Comparison of the deduced amino acid sequence with amino acid sequence databanks revealed a strong homology with glutathione S-transferases. The nucleotide sequence of the clone displayed a strong homology with the active glutathione binding site of glutathione transferases and contained all but one of the 19 positionally conserved amino acid residues found in glutathione transferases. The cloned polypeptide was expressed in Escherichia coli and affinity-purified on glutathione agarose.
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页码：521 / 528
页数：8
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