AMINO-TERMINAL BLOCKING GROUP AND SEQUENCE OF THE ANIMAL FATTY-ACID SYNTHASE

被引:14
|
作者
HUANG, WY [1 ]
CHIRALA, SS [1 ]
WAKIL, SJ [1 ]
机构
[1] BAYLOR COLL MED,VERNA & MARRS MCLEAN DEPT BIOCHEM,HOUSTON,TX 77030
关键词
D O I
10.1006/abbi.1994.1410
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
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. (C) 1994 Academic Press, Inc.
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页码:45 / 49
页数:5
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