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

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.

1982 ◽  
Vol 94 (2) ◽  
pp. 251-NP ◽  
Author(s):  
Janet M. Nolin ◽  
Betty J. Thompson ◽  
Stuart Smith

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.


Biochemistry ◽  
1987 ◽  
Vol 26 (5) ◽  
pp. 1358-1364 ◽  
Author(s):  
Richard Safford ◽  
Jacquie De Silva ◽  
Clare Lucas ◽  
John H. C. Windust ◽  
James Shedden ◽  
...  

1989 ◽  
Vol 17 (5) ◽  
pp. 886-887 ◽  
Author(s):  
ANTONI R. SLABAS ◽  
ALASTAIR AITKEN ◽  
STEVEN HOWELL ◽  
KEVIN WELHAM ◽  
CHRISTOPHER M. SIDEBOTTOM

1981 ◽  
Vol 114 (3) ◽  
pp. 643-651 ◽  
Author(s):  
John S. MATTICK ◽  
Zendra E. ZEHNER ◽  
Michael A. CALABRO ◽  
Salih J. WAKIL

1982 ◽  
Vol 202 (1) ◽  
pp. 139-143 ◽  
Author(s):  
J Knudsen ◽  
I Grunnet

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.


1976 ◽  
Vol 160 (3) ◽  
pp. 683-691 ◽  
Author(s):  
J Knudsen ◽  
S Clark ◽  
R Dils

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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