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Titlebook: Esterases, Lipases, and Phospholipases; From Structure to Cl M. I. Mackness,M. Clerc Book 1994 Springer Science+Business Media New York 199

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书目名称Esterases, Lipases, and Phospholipases
副标题From Structure to Cl
编辑M. I. Mackness,M. Clerc
视频video
丛书名称NATO Science Series A:
图书封面Titlebook: Esterases, Lipases, and Phospholipases; From Structure to Cl M. I. Mackness,M. Clerc Book 1994 Springer Science+Business Media New York 199
描述The NATO-Advanced Research Workshop "Esterases, Lipases and Phospholipases: From Structure to Clinical Significance" was held at the University of Bordeaux II, France from 22nd- 24th September 1993 under the Directorship of Professor Michel Clerc of the University of Bordeaux II. The meeting was organised by Hugues Chap (INSERM U 326, Toulouse, France), Georges Ferard (University of Strasbourg, France), Wolfgang Junge (University of Kiel, Germany) and Michael Mackness (University of Manchester, UK). In recent years it has become increasingly apparent that hydrolytic enzymes of the esterase, lipase and phospholipase type play central roles in the pathophysiology of many human diseases. The purpose of this NATO-ARW was to bring together experts (both clinical and scientific) in all three interrelated fields to review the current basic and clinical position and discuss future developments particularly with respect to future research aimed at determining the basic biochemical lesion involving hydrolytic enzymes involved in human disease and the use of these enzymes in diagnosis. As well as formal lectures from established researchers, the meeting also involved a number of lively round-
出版日期Book 1994
关键词Diabetes; Lipid; biochemistry; enzymes; metabolism; proteins
版次1
doihttps://doi.org/10.1007/978-1-4899-0993-0
isbn_softcover978-1-4899-0995-4
isbn_ebook978-1-4899-0993-0
copyrightSpringer Science+Business Media New York 1994
The information of publication is updating

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发表于 2025-3-21 22:44:53 | 显示全部楼层
Douglas J. Loveless,Bryant Griffithe feeding of a cholesterol-rich diet causes an increased activity of serum total esterase in rats, rabbits and mice. Cholesterol loading of rats, but not rabbits, lowers serum butyrylcholinesterase activity. The activity or level of a fast anodal serum esterase zone in rats (ES-1) and mice (ES-2) is
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Co-creation in Nurse Education,and xenobiotics. Carboxylesterases act also, in vitro, on endogenous lipid substrates, but the physiological meaning of their action on these compounds is still unclear [1, 2]. Most liver carboxylesterases reside in the lumen of the endoplasmic reticulum (ER) where they are either free, or loosely b
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Wai Fong Chua,Tony Lowe,Tony Puxtyty and one with high activity. Paraoxonase prevents lipid peroxide generation during the Cu. catalysed oxidation of LDL . and may therefore contribute to the . protection by HDL against the development of atherosclerosis. The presence of different allozymes of paraoxonase in the population may contr
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https://doi.org/10.1007/978-3-030-53728-9issue and are of the serine hydrolase type, but activation experiments with Ca. point to a possible involvement of epidermal phospholipase A2 in the hydrolysis of myristoyl esters and especially of sorbitan trioleate. Fatty acid ethyl and propyl esters, and 4hydroxy-benzoic acid esters are degraded
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https://doi.org/10.1057/9781137294104 to the inhibitor diisopropylfluorophosphate classifies this enzyme as a carboxylesterase with a serine residue at the active site which is involved in hydrolysis. ANA cleaving enzymes are also present in other haematopoietic cells. Isoelectric focusing of proteins from purified haemapoietic cells r
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The Challenges of Disablist Hate CrimeAs pointed out by E. Reiner this becomes particularly evident within the two groups of enzymes reacting with organophosporous compounds, i.e. phosphotriester hydrolases (EC 3.1.8) and the “true” carboxylesterases like EC 3.1.1.1 or cholinesterase (3.1.1.8). Organophosphates are substrates of the for
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