Title of article :
Amino-Terminal Blocking Group and Sequence of the Animal Fatty Acid Synthase
Author/Authors :
Huang، نويسنده , , W.Y. and Chirala، نويسنده , , S.S. and Wakil، نويسنده , , S.J.، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 1994
Pages :
5
From page :
45
To page :
49
Abstract :
We have cloned and sequenced the cDNA encoding the chicken fatty acid synthase. Based on the nucleotide-derived amino acid sequence of the chicken synthase, the N-terminal sequences are highly conserved among animal species, suggesting that translation of the animal synthases initiates with the same ATG codon. Like other fatty acid synthases, the NH2-terminal sequence of the chicken enzyme is blocked. We have isolated and purified the blocked NH2-terminal peptide from a tryptic digest of chicken synthase and have established that the blocking group is an acetyl group. The sequence of the native tryptic peptide confirmed the cDNA-derived amino acid sequence and suggested that all animal synthases begin with this homologous sequence. We developed simple procedures that can be used to isolate and characterize any blocked NH2-terminal peptide.
Journal title :
Archives of Biochemistry and Biophysics
Serial Year :
1994
Journal title :
Archives of Biochemistry and Biophysics
Record number :
1452389
Link To Document :
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