Title of article :
Molecular Evolution of Amphioxus Fructose-1,6- bisphosphate Aldolase
Author/Authors :
Kuba، نويسنده , , Masako and Yatsuki، نويسنده , , Hitomi and Kusakabe، نويسنده , , Takahiro and Takasaki، نويسنده , , Yozo and Nikoh، نويسنده , , Naruo and Miyata، نويسنده , , Takashi and Yamaguchi، نويسنده , , Takao and Hori، نويسنده , , Katsuji، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 1997
Pages :
8
From page :
329
To page :
336
Abstract :
The cDNA for amphioxus fructose-1,6-bisphosphate (FBP)-aldolase was isolated and its nucleotide sequence was determined. In the cDNA, there existed a probable open reading frame comprising 1080 bp; hence, 359 amino acid residues were deduced. The amino acid sequence indicates the deletion of 4 residues from N-terminus, in comparison with the sequence of FBP-aldolase isozymes from other sources. There was only one FBP-aldolase gene, and one enzyme species corresponding, in the amphioxus; this is the first report of the existence of a single FBP-aldolase species in animals. Enzymatic studies of both native and the recombinant FBP-aldolase suggest that the amphioxus enzyme belongs to an ancestral class I type which is not discovered among vertebrate aldolase isozymes.
Keywords :
Evolution , Amphioxus , aldolase , Isozyme , Purification , characterization
Journal title :
Archives of Biochemistry and Biophysics
Serial Year :
1997
Journal title :
Archives of Biochemistry and Biophysics
Record number :
1609670
Link To Document :
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