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Titlebook: Gene-Enzyme Systems in Drosophila; William J. Dickinson,David T. Sullivan Book 1975 Springer-Verlag Berlin Heidelberg 1975 Drosophila.Enzy

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書目名稱Gene-Enzyme Systems in Drosophila
編輯William J. Dickinson,David T. Sullivan
視頻videohttp://file.papertrans.cn/383/382011/382011.mp4
叢書名稱Results and Problems in Cell Differentiation
圖書封面Titlebook: Gene-Enzyme Systems in Drosophila;  William J. Dickinson,David T. Sullivan Book 1975 Springer-Verlag Berlin Heidelberg 1975 Drosophila.Enzy
描述There was a period in the history of modern biology when proteins were thought to be "gene products" in a rather direct sense. An account of their appearance and disappearance in the course of development and differentiation thus seemed an appropriate means of describing "gene regulation". When RNA was found to be the immediate product of genetic activity, the study of proteins as gene products lost some of its original attraction. Indeed, the development of the powerful method of nucleic acid hybridization aroused the hope that a large array of specific messenger-RNA molecules synthesized during cell differentiation could be individually assayed. The difficulties in the way of such ambitious projects were described in Volume 3 of this series: Nucleic Acid Hybridization in the Study of Cell Differentiation (ed. H. URSPRUNG, 1972). Enzymes are in large measure responsible for cell function. Clearly, their synthesis must be under genetic control. We are convinced that the study of enzyme behavior during development merits much attention, particularly if the work is carried out on a eukaryote that lends itself to genetic and developmental analysis. An impressive amount of genetic info
出版日期Book 1975
關鍵詞Drosophila; Enzym; Enzyme; Molekulargenetik; Sullivan; Zelldifferenzierung; proteins; regulation
版次1
doihttps://doi.org/10.1007/978-3-540-37283-7
isbn_softcover978-3-662-21942-3
isbn_ebook978-3-540-37283-7Series ISSN 0080-1844 Series E-ISSN 1861-0412
issn_series 0080-1844
copyrightSpringer-Verlag Berlin Heidelberg 1975
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Dehydrogenases,chemical and genetic studies because of the availability of a rapid, sensitive, quantitative assay, and a histochemical method of detection that has been readily adapted to electrophoretic supporting media allowing for the screening of electrophoretic variants (Fig. 21). The quantitative assay is de
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Non-Specific Hydrolytic Enzymes,antage of artificial substrates, such as L-leucyl-β-naphthylamide, using diazonium salts to trap the naphthol released by enzymatic cleavage (. and ., 1964c). A few studies have used natural proteins as substrate, and determine general proteolytic activity in terms of amino acids (e.g., tyrosine) re
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Miscellaneous Enzymes,us dissaccharides and trissaccharides by crude extracts has shown that enzymatic activity is specific for the glucosidic linkage. The rate of hydrolysis of sucrose is about four times that of trehalose. Melezitose, turnanose and maltose are cleaved at slower rates. Crude extracts do not hydrolyze me
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