The Isolation and Characterization of Fatty-Acid-Synthetase mRNA from Rat Mammary Gland

1981 ◽  
Vol 114 (3) ◽  
pp. 643-651 ◽  
Author(s):  
John S. MATTICK ◽  
Zendra E. ZEHNER ◽  
Michael A. CALABRO ◽  
Salih J. WAKIL
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Fatty Acid Synthetase ◽  
Isolation And Characterization ◽  
Rat Mammary Gland

Molecular cloning and sequence analysis of complementary DNA encoding rat mammary gland medium-chain S-acyl fatty acid synthetase thio ester hydrolase

Biochemistry ◽  
1987 ◽  
Vol 26 (5) ◽  
pp. 1358-1364 ◽  
Author(s):  
Richard Safford ◽  
Jacquie De Silva ◽  
Clare Lucas ◽  
John H. C. Windust ◽  
James Shedden ◽  
...  
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Sequence Analysis ◽  
Molecular Cloning ◽  
Fatty Acid Synthetase ◽  
Dna Encoding ◽  
Complementary Dna ◽  
Medium Chain ◽  
Ester Hydrolase ◽  
Rat Mammary Gland

scholarly journals Release of two thioesterase domains from fatty acid synthetase by limited digestion with trypsin

1978 ◽  
Vol 175 (1) ◽  
pp. 199-206 ◽  
Author(s):  
K N Dileepan ◽  
C Y Lin ◽  
S Smith
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Active Sites ◽  
Fatty Acid Synthetase ◽  
Trypsin Treatment ◽  
Major Species ◽  
Rat Mammary Gland ◽  
Limited Digestion ◽  
A Minor

Limited digestion, with trypsin, of the fatty acid synthetase from rat mammary gland releases an enzymically active thioesterase component that, under denaturing conditions, consists of two major species of mol.wts. 35000 and 17500 and a minor species, mol.wt. 15,000. The 17500- and 150000-mol.wt. species are shown to originate from the 35000-mol.wt. species as a result of nicking by trypsin. The nicked polypeptides are enzymically active. The fatty acid synthetase is inhibited by [1,3-14C]di-isopropyl phosphorofluoridate, which is shown to bind to, and inactivate, two thioesterase active sites. When the [1,3-14C]di-isopropyl phosphate-labelled fatty acid synthetase is subjected to limited digestion with trypsin, all of the radioactivity is recovered in the isolated thioesterase component, i.e. in the 35000-mol.wt. polypeptide and its nicked products. Since the isolated thioesterase is shown to bind only one di-isopropyl phosphate residue per 35000-mol.wt. polypeptide, we conclude that the fatty acid synthetase has two thioesterase domains, both of which are removed by limited trypsin treatment.

scholarly journals Cloning and sequencing of the medium-chain S-acyl fatty acid synthetase thioester hydrolase cDNA from rat mammary gland

1987 ◽  
Vol 243 (2) ◽  
pp. 597-601 ◽  
Author(s):  
J Naggert ◽  
B Williams ◽  
D P Cashman ◽  
S Smith
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Fatty Acid Synthetase ◽  
Cdna Clones ◽  
Amino Acid Residues ◽  
Coding Region ◽  
Enzyme Active Site ◽  
Medium Chain ◽  
Thioesterase Ii ◽  
Rat Mammary Gland

cDNA clones coding for the medium-chain S-acyl fatty acid synthetase thioester hydrolase (thioesterase II) from rat mammary gland were identified in a bacteriophage lambda gt11 library and their nucleotide sequences were determined. The predicted coding region spans 263 amino acid residues and includes a sequence identical with that of a peptide derived from the enzyme active site. The rat thioesterase II cDNA sequence exhibits homology with that of a thioesterase found in duck uropygial glands.

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