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Titlebook: Control of Enzyme Activity; Philip Cohen Book 1983 P. Cohen 1983 Nucleotide.amino acid.bacteria.biology.enzyme.enzymes.phosphorylation.syn

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發(fā)表于 2025-3-21 18:30:31 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書目名稱Control of Enzyme Activity
編輯Philip Cohen
視頻videohttp://file.papertrans.cn/238/237368/237368.mp4
叢書名稱Outline Studies in Biology
圖書封面Titlebook: Control of Enzyme Activity;  Philip Cohen Book 1983 P. Cohen 1983 Nucleotide.amino acid.bacteria.biology.enzyme.enzymes.phosphorylation.syn
描述The student of biological science in his final years as an undergraduate and his first years as a graduate is expected to gain some familiarity with current research at the frontiers of his discipline. New research work is published in a perplexing diversity of publications and is inevitably concerned with the minutiae of the subject. The sheer number of research journals and papers also causes confusion and difficulties of assimilation. Review articles usually presuppose a background knowledge of the field and are inevitably rather restricted in scope. There is thus a need for short but authoritative introductions to those areas of modern biological research which are either not dealt with in standard introductory textbooks or are not dealt with in sufficient detail to enable the student to go on from them to read scholarly reviews with profit. This series of books is designed to satisfy this need. The authors have been asked to produce a brief outline of their subject assuming that their readers will have read and remembered much of a standard introductory textbook of biology.
出版日期Book 1983
關(guān)鍵詞Nucleotide; amino acid; bacteria; biology; enzyme; enzymes; phosphorylation; synthesis
版次1
doihttps://doi.org/10.1007/978-94-009-5981-1
isbn_softcover978-0-412-25560-1
isbn_ebook978-94-009-5981-1
copyrightP. Cohen 1983
The information of publication is updating

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The nature of the allosteric transition,re still very tentative. In the case of ATCase there is some evidence that the transition from an active to an inactive state involves a small molecular expansion of the enzyme, and the preservation of the C:R-R:C unit (Fig. 2.12) implies that some change in the twist of the catalytic subunit . relative to the regulatory subunit . must take place.
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發(fā)表于 2025-3-22 11:54:43 | 只看該作者
Book 1983t with in sufficient detail to enable the student to go on from them to read scholarly reviews with profit. This series of books is designed to satisfy this need. The authors have been asked to produce a brief outline of their subject assuming that their readers will have read and remembered much of a standard introductory textbook of biology.
6#
發(fā)表于 2025-3-22 15:23:48 | 只看該作者
ity with current research at the frontiers of his discipline. New research work is published in a perplexing diversity of publications and is inevitably concerned with the minutiae of the subject. The sheer number of research journals and papers also causes confusion and difficulties of assimilation
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Enzyme regulation by reversible phosphorylation: the neural and hormonal control of cellular activier the period 1955–1970, when they discovered that the neural and hormonal control of glycogen metabolism was mediated by changes in the phosphorylation state of glycogen phosphorylase [1], phosphorylase kinase [2] and glycogen synthase [3].
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發(fā)表于 2025-3-23 07:41:30 | 只看該作者
Regulation of amino acid and nucleotide biosynthesis in bacteria by end product inhibition,tion had already centred on how these reactions might be regulated to make the most effective use of available nutrients. Indeed, many of the isotopic and mutant studies which had been used to elucidate the sequence of steps in these pathways had themselves given the first clues as to how these cont
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