Crystallization and preliminary diffraction studies of thioesterase II from rat mammary gland

1995 ◽  
Vol 22 (1) ◽  
pp. 73-75 ◽  
Author(s):  
Jenny L. Buchbinder ◽  
Andrzej Witkowski ◽  
Stuart Smith ◽  
Robert J. Fletterick
Keyword(s):  
Mammary Gland ◽  
Thioesterase Ii ◽  
Rat Mammary Gland

scholarly journals A catalytic role for histidine 237 in rat mammary gland thioesterase II.

1991 ◽  
Vol 266 (28) ◽  
pp. 18514-18519 ◽  
Author(s):  
A. Witkowski ◽  
J. Naggert ◽  
B. Wessa ◽  
S. Smith
Keyword(s):  
Mammary Gland ◽  
Thioesterase Ii ◽  
Catalytic Role ◽  
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.

Identification of the N-terminal blocking group of rat mammary gland acyl fatty acid synthetase-thioesterase II

1989 ◽  
Vol 17 (5) ◽  
pp. 886-887 ◽  
Author(s):  
ANTONI R. SLABAS ◽  
ALASTAIR AITKEN ◽  
STEVEN HOWELL ◽  
KEVIN WELHAM ◽  
CHRISTOPHER M. SIDEBOTTOM
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Fatty Acid Synthetase ◽  
Blocking Group ◽  
Thioesterase Ii ◽  
Rat Mammary Gland
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