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 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.

Localization of thioesterase II, the chain-length regulatory enzyme of milk fatty acid synthesis, in rat mammary gland epithelial cells

1982 ◽  
Vol 94 (2) ◽  
pp. 251-NP ◽  
Author(s):  
Janet M. Nolin ◽  
Betty J. Thompson ◽  
Stuart Smith
Keyword(s):  
Fatty Acids ◽  
Mammary Gland ◽  
Fatty Acid ◽  
Epithelial Cells ◽  
Fatty Acid Synthetase ◽  
Medium Chain ◽  
Medium Chain Fatty Acids ◽  
Thioesterase Ii ◽  
Rat Mammary Gland ◽  
Chain Fatty Acids

Two approaches were used to establish the intercellular distribution of fatty acid synthetase and thioesterase II in the lactating rat mammary gland. Thioesterase II is the chain-length regulatory enzyme in the biosynthesis of the medium-chain fatty acids characteristic of milk fat. Using immunohistochemical techniques, immunoreactive fatty acid synthetase was found in both mammary adipocytes and epithelial cells; in contrast, immunoreactive thioesterase II was confined to the epithelial cells. In metabolic studies, adipocytes and epithelial cells were isolated from lactating rat mammary glands after digestion with collagenase and thermolysin, and their lipogenic activity was studied using isotopically labelled acetate. Consistent with the immunohistochemical data, adipocytes synthesized exclusively long-chain fatty acids whereas epithelial cells synthesized predominantly medium-chain fatty acids. The results indicate that the capacity for synthesis of medium-chain fatty acids is a unique property of the epithelial cell component of the mammary gland.

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

scholarly journals Transacylation as a chain-termination mechanism in fatty acid synthesis by mammalian fatty acid synthetase. Synthesis of medium-chain-length (C8-C12) acyl-CoA esters by goat mammary-gland fatty acid synthetase

1982 ◽  
Vol 202 (1) ◽  
pp. 139-143 ◽  
Author(s):  
J Knudsen ◽  
I Grunnet
Keyword(s):  
Fatty Acids ◽  
Mammary Gland ◽  
Fatty Acid ◽  
Fatty Acid Synthetase ◽  
Acid Synthesis ◽  
Medium Chain ◽  
Medium Chain Fatty Acids ◽  
Medium Chain Length ◽  
A Chain ◽  
Chain Fatty Acids

1. Ruminant mammary-gland fatty acid synthetases can, in contrast with non-ruminant mammary enzymes, synthesize medium-chain fatty acids. 2. Medium-chain fatty acids are only synthesized in the presence of a fatty acid-removing system such as albumin, beta-lactoglobulin or methylated cyclodextrin. 3. The short- and medium-chain fatty acids synthesized were released as acyl-CoA esters from the fatty acid synthetase.

scholarly journals Purification and some properties of a medium-chain acyl-thioester hydrolase from lactating-rabbit mammary gland which terminates chain elongation in fatty acid synthesis

1976 ◽  
Vol 160 (3) ◽  
pp. 683-691 ◽  
Author(s):  
J Knudsen ◽  
S Clark ◽  
R Dils
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Fatty Acid Synthetase ◽  
Acid Synthesis ◽  
Chain Elongation ◽  
Medium Chain ◽  
Chain Acyl

1. An acyl-thioester hydrolase was isolated from the cytosol of lactating-rabbit mammary gland. The purified enzyme terminates fatty acid synthesis at medium-chain (C8:0-C12:0) acids when it is incubated with fatty acid synthetase and rate-limiting concentrations of malonyl-CoA. These acids are characteristic products of the lactating gland. 2. The mol.wt. of the enzyme is 29000±500 (mean±S.D. of three independent preparations), as estimated by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. 3. The enzyme also hydrolyses acyl-CoA esters of chain lengths C10:0-C16:0 when these are used as model substrates. The greatest activity was towards dodecanoyl-CoA, and the three preparations had specific activities of 305, 1130 and 2010 nmol of dodecanoyl-CoA hydrolysed/min per mg of protein when 56muM substrate was used. 4. The way in which this enzyme controls the synthesis of medium-chain fatty acids by fatty acid synthetase is briefly discussed.

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