酶動力學(xué)

內(nèi)容概要

本書介紹并闡明了使酶科學(xué)興旺發(fā)達(dá)一個多世紀(jì)的酶學(xué)原理及其最好的實驗技術(shù)。為了便于分子生命科學(xué)家、化學(xué)家、物理學(xué)家和工程師全面參與。本書開辟了化學(xué)動力學(xué)、活性部位化學(xué)、酶分析技術(shù)和抑制劑設(shè)計等方面的論題。本書引用了2600多篇經(jīng)典的和現(xiàn)代文獻。重點放在穩(wěn)態(tài)動力學(xué)和瞬態(tài)動力學(xué)上。書中前所未有的一章是單分子酶動力學(xué)和生物力產(chǎn)生，因此，對生物化學(xué)、化學(xué)、分子生物學(xué)、生物工程學(xué)、藥物學(xué)、植物科學(xué)和化學(xué)工程學(xué)等方面的研究生和高級研究人員來說，本書是最新、最詳盡的單卷本酶學(xué)參考書。

作者簡介

作者：(美國)丹尼爾?L?普里策(Daniel L. Purich)

書籍目錄

第一章　酶學(xué)導(dǎo)論
第二章　活性部位及其化學(xué)性質(zhì)
第三章　化學(xué)動力學(xué)基礎(chǔ)
第四章　測寫初始速度和瓜參數(shù)的實際考考慮
第五章　單底物酶催化反應(yīng)的始速度動力學(xué)
第六章　多底物酶催化反應(yīng)的初始速度動力學(xué)
第七章　影響酶活力的因素
第八章　酶抑制劑的動力學(xué)行力
第九章　用同位素檢測生物催化作用
第十章　檢測快速酶過程
第十一章　酶的調(diào)節(jié)行為
第十二章　單分子酶動力學(xué)
第十三章　機械力酶：催化、力的產(chǎn)生和動力學(xué)
參考文獻
附錄
術(shù)語表
索引

章節(jié)摘錄

版權(quán)頁：插圖：to show that the rate of this reaction is linearly dependenton the concentration of sugar. Berthelot （1862） and Berthelot and de Saint-Gilles （1862） reached the same cnclusion from studies on e.thyl acetate hydrolysis, and   such observations led Guldberg and Waage （1867; 1979） to  postulate that chemical reactions must be highly dynamic, with reactants and products relentlessly interconverting into each other, even at equilibrium. In advancing this principle, widely known as the Law of Mass Action, they suggested that the rate in each direction of a reversiblereaction depends on reactant concentration （often expressed as the intensive variable molarity） and not the amount of substance （commonly given by the extensive variable mole）. . As discussed at length in Chapter 3, the modernconceptual framework for the discipline known aschemical kinetics was founded late in the nineteenth century by the powerfully insightful contributions of theSwedish chemist Svante Arrhenius and the Germanchemist Jacob van't Hoff, who both became NobelLaureates 2in,chemistry. They and.German physical chemist Wilhelm Ostwald, the Nobelist credited for firstexpressmg reaction velocity as a change in reactant concentration per unit time （i.e., v = -d[Reactant]/dt）,established the enduring concept that catalysts promote reactivity without altering the equilibrium position of the overall chemical reaction. These investigators recognizedthat thermodynamics constrains catalysis: after eachcatalytic round, the catalyst releases its product andtherefore cannt exert any cumulative effect on the reaction's standard Gibbs free energy change AGo. Thisdiscovery increased the determination of chemists to discover catalytic substances and even to design artificialcatalysts endowed with special properties. Speed and yield are the essence of catalysis, but the idea that one may impart reactivity to otherwise unreactive substances  lies at the heart of modern chemical enterprises. Nowhere is this more evident than in the Work of Fritz Haber, thenotorious German chemical engineer5 and NobelLaureate. Haber's research team overcame the virtualinertness of dinitrogen by carrying out some 20,000 experiments, utilizing thousands of catalyst preparations under a wide range of reaction conditions. They eventu-  ally settled on the use of iron filings to catalyze ammonia synthesis from N2 and H2 at high temperature （600-800K） and extreme pressure （300 atm）.

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《酶動力學(xué):催化作用和調(diào)控作用(導(dǎo)讀版)(英文版)》由科學(xué)出版社出版。

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