منابع مشابه
Cholesterol esterases: IV. Cholesterol esterase of rat intestinal mucosa.
Nieft and Deuel (1, 2) found that in rat liver and intestinal mucosa two different opposing systems were responsible for the synthesis and hydrolysis of cholesterol esters. The esterifying system required the presence of phosphate ion and a fatty acid source. The hydrolytic system consisted of at least two factors and its activity was accentuated by soy bean lecithin. While their extracts were ...
متن کاملContinuous monitoring of cholesterol oleate hydrolysis by hormone-sensitive lipase and other cholesterol esterases.
Hormone-sensitive lipase (HSL) contributes importantly to the hydrolysis of cholesteryl ester in steroidogenic tissues, releasing the cholesterol required for adrenal steroidogenesis. HSL has broad substrate specificity, because it hydrolyzes triacylglycerols (TAGs), diacylglycerols, monoacylglycerols, and cholesteryl esters. In this study, we developed a specific cholesterol esterase assay usi...
متن کاملCholesterol esterases; preparation of substrate mixture and characterization of the hydrolytic cholesterol and esterase of pancreatin.
The enzyme or enzymes involved in the formation and hydrolysis of cholesterol esters have been the subject of sporadic studies since 1910 when Kondo (1) reported that extracts of horse and ox liver catalyzed the hydrolysis of these esters. The most extensive studies have been carried out by Sperry and coworkers (2) who also reviewed the earlier literature and pointed out the lack of agreement b...
متن کاملEsterases Reacting with Organophosphorus Compounds
The sixty-seven papers in this book are grouped under the following chapters: Esterase Structures, Catalytic Properties of Cholinesterases, Catalytic Properties of Paraoxonases and Related Esterases, Biology of Cholinesterases, Biology of Paraoxonases and Related Esterases, Toxicity and Degradation of Organophosphorus Compounds, Neuropathy Target Esterase, and Miscellaneous. The chapters are pr...
متن کاملOn the origins of esterases.
Comparisons among the primary sequences of five cloned eukaryotic esterases reveal two distinct lineages, neither bearing any significant overall sequence similarity to the functionally related serine protease multigene family. We have not eliminated the possibility that the esterases may have residual conformational similarities to the serine proteases. However, our profile analysis and analys...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1953
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)77272-x