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Titlebook: Diabetes and Protein Glycosylation; Measurement and Biol Margo Panush Cohen Book 1986 Springer-Verlag New York Inc. 1986 Diabetes.G protein

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發(fā)表于 2025-3-21 17:28:58 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書目名稱Diabetes and Protein Glycosylation
副標(biāo)題Measurement and Biol
編輯Margo Panush Cohen
視頻videohttp://file.papertrans.cn/271/270424/270424.mp4
圖書封面Titlebook: Diabetes and Protein Glycosylation; Measurement and Biol Margo Panush Cohen Book 1986 Springer-Verlag New York Inc. 1986 Diabetes.G protein
描述In the years since the initial discovery that blood from diabetic patients contains increased amounts of a posttranslationally gluco- sylated form of hemoglobin (hemoglobin Ale)‘ an impressive number of studies have clarified and expanded the use of glycohemoglobin levels to assess disease status. Many other structural proteins have been shown to undergo similar changes, including proteins from tissues most commonly affected in diabetes (e.g., lens, aorta, peripheral nerve, basement membrane). Thus, the nonenzymatic glycosylation of hemoglobin emerges as an invaluable model for the pathogenesis of certain chronic diabetes complications. In addition to reviewing a wealth of investigative possibilities in the area of these chronic complications-including eye, kidney, nerve, and vascular disease-Dr. Cohen indicates how enhanced nonenzymatic glycosylation in uncontrolled diabetes underscores the pressing need for maintenance of long-term euglycemia. Dr. Cohen is an endocrinologist and diabetes specialist whose research activities have largely focused on the chemistry and metabo- lism of the basement membrane in diabetes. This superb monograph on nonenzymatic glycosylation clearly shows
出版日期Book 1986
關(guān)鍵詞Diabetes; G proteins; Monosaccharid; enzymes; proteins; tissue; translation; metabolic disease
版次1
doihttps://doi.org/10.1007/978-1-4612-4938-2
isbn_softcover978-1-4612-9366-8
isbn_ebook978-1-4612-4938-2
copyrightSpringer-Verlag New York Inc. 1986
The information of publication is updating

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Oliver Gassmann,Fiona Schweitzerred cells of diabetic patients, the oxygen affinity of these cells in the presence of 2,3-DPG is slightly greater than that of red cells from nondiabetic subjects.. This difference could be explained on the basis of the interference presented by the NH.-terminal glucose of Hb A. to the binding of 2,3-DPG.
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Book 1986hemoglobin (hemoglobin Ale)‘ an impressive number of studies have clarified and expanded the use of glycohemoglobin levels to assess disease status. Many other structural proteins have been shown to undergo similar changes, including proteins from tissues most commonly affected in diabetes (e.g., le
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Chemistry,a 1-amino-l-deoxyfructose derivative in stable ketoamine linkage, which in turn can cyclize to a ring structure.. This bimolecular condensation of free saccharide with protein constitutes a mechanism by which proteins are subjected to postribosomal modification without the influence of enzymatic activities.
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Handbuch Energiewende und Partizipationcirculating proteins such as hemoglobin and albumin, thus allowing measurement of glycohemoglobin or glycoalbumin to be used for assessing diabetic control, but also of tissue proteins, thereby providing insight into pathogenetic mechanisms contributory to chronic complications of diabetes.
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