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Titlebook: Enzymology and Molecular Biology of Carbonyl Metabolism 3; Henry Weiner,Bendicht Wermuth,David W. Crabb Book 1991 The Editor(s) (if applic

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书目名称Enzymology and Molecular Biology of Carbonyl Metabolism 3
编辑Henry Weiner,Bendicht Wermuth,David W. Crabb
视频video
丛书名称Advances in Experimental Medicine and Biology
图书封面Titlebook: Enzymology and Molecular Biology of Carbonyl Metabolism 3;  Henry Weiner,Bendicht Wermuth,David W. Crabb Book 1991 The Editor(s) (if applic
描述The Fifth International Workshop on the Enzymology and Molecular Biology of Carbonyl Metabolism was held at Purdue University in June, 1990. This represents the fifth time that I had the privilege of organizing the scientific program. It was the first time that I actually hosted the meeting. I wish to salute my four previous co-organizers and the thousands of scientists who have hosted other meetings. It is much easier to arrange the scientific program and edit the proceedings. No local organization could occur without the help of ones research group and, in this case, my wife. I sincerely thank Esther and my research group for their advise and help. At this Workshop, similar to the preceeding ones, much new information was presented. It was apparent how molecular biological techniques were influencing the direction of the research on the three families of enzymes discussed. It also was apparent that not all biochemical problems could be solved by using these techniques. Many of the presentations showed how important advances still could be made using more traditional biochemical approaches.
出版日期Book 1991
关键词biology; carbon; enzymes; enzymology; metabolism; molecular biology; research
版次1
doihttps://doi.org/10.1007/978-1-4684-5901-2
isbn_softcover978-1-4684-5903-6
isbn_ebook978-1-4684-5901-2Series ISSN 0065-2598 Series E-ISSN 2214-8019
issn_series 0065-2598
copyrightThe Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Science+Busines
The information of publication is updating

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Localization of Cysteine 302 at the Active Site of Aldehyde Dehydrogenaseart of 35 residue tryptic peptide (Hempel, 1981; Hempel and Pietruszko, 1981; Hempel et al., 1982) by employing iodoacetamide. When the primary structures of the El and E2 isozymes were established (Hempel et al., 1984, 1985; Hsu et al., 1985), this cysteine was found to occupy position 302 in a 500
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PH Effects on Cytoplasmic Aldehyde Dehydrogenase from Sheep Livergive a complete picture of the mechanism of the aldehyde dehydrogenase catalyzed oxidation of propionaldehyde over an extended pH range. The enzyme catalyzed oxidation reaction at pH 7.0 and 7.6 is generally agreed to occur by the following ordered mechanism:.Scheme IAt least at low propionaldehyde
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Biochemical, Immunological, and Molecular Characterization of a “High KM” Aldehyde Dehydrogenaseportant role in the toxic consequences of a deranged acetaldehyde metabolism in alcohol-related disorders (Agarwal and Goedde, 1989, 1990; Goedde and Agarwal, 1989). Two broadly defined groups of ALDHs have been recognized based upon their Michaelis constants (“low Km” and “high Km” isozymes). The m
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Purification and Properties of Baboon Corneal Aldehyde Dehydrogenase: Proposed UVR Protective Roleal cells and the lens, by the absorption of UVR in the 290–320 nm wavelength range (UV-B) (Boettner and Wolters, 1962; Zigman, 1983). The mechanisms of corneal photoreception of UV-B light have not been determined, as yet, although studies examining the action spectra for the cornea in the induction
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Metabolism of 4-Hydroxynonenal in Hepatoma Cell Linesidation is well regulated and, as noted in a recent review (Esterbauer. et al. , 1990), is always associated with the formation of numerous and chemically diverse aldehydic products. Malondialdehyde (MDA) and trans-4-hydroxy-2-nonenal (HNE) are classified as major products of lipid peroxidation sinc
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