Title of article :
Characterization of a Pollination-Related cDNA fromPhalaenopsisEncoding a Protein Which Is Homologous to Human Peroxisomal Acyl-CoA Oxidase
Author/Authors :
Do، نويسنده , , Yi-Yin and Huang، نويسنده , , Pung-Ling، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 1997
Pages :
6
From page :
295
To page :
300
Abstract :
The first putative plant acyl-CoA oxidase cDNA has been isolated from aPhalaenopsiscDNA library constructed by poly(A)+RNA extracted from petals 1 day after pollination. This cDNA, pOACO31, contains a 2100-bp open reading frame which encodes a polypeptide named PACO1 of 699 amino acids. The predicted isoelectric point of PACO1 is 8.74 and the molecular weight is 78,032 Da, similar to that of a monomer of predicted plant acyl-CoA oxidase. Southern blot analysis indicated that this gene occurs in one copy or a low number of copies per haploid genome. When compared with sequences in databases, PACO1 revealed significant similarity only to peroxisomal acyl-CoA oxidase particularly within 13 conserved regions and a putative FMN-binding site.
Keywords :
peroxisomal acyl-CoA oxidase homolog , Petal senescence , Phalaenopsis.
Journal title :
Archives of Biochemistry and Biophysics
Serial Year :
1997
Journal title :
Archives of Biochemistry and Biophysics
Record number :
1609285
Link To Document :
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