Kinetic mechanism and enzyme function.

نویسنده

  • K F Tipton
چکیده

never visited America, and his two periods of sabbatical leave from Cambridge University were spent at the Molten0 Institute of Parasitology and at King’s College, respectively 100 and 400 metres from the Department of Biochemistry. In the years leading up to his official retirement in 1966, and in the years following, Malcolm Dixon continued to pursue research, usually, as had been his custom, carrying out all the stages himself. He had only had a personal laboratory assistant for five of his years of research, and had never had a secretary-all his writing being typed personally on an ancient but immaculate typewriter. His active Christianity and his interest in music (he is a most accomplished pianist) have provided him with a lifelong circle of friends. He is held in great esteem by several generations of biochemical students who have passed through Cambridge, by all those who have been his personal students or colleagues and by enzymologists throughout the world who may know him only through his published work. It is very pleasant to note that his eightieth year has been marked, not only by appropriate ceremonies, but also by the publication of the third edition of ‘Enzymes’, the work for which had occupied Malcolm Dixon for much of his, and the century’s, seventies.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

In Vitro Inhibition of Human Sperm Creatine Kinase by Nicotine, Cotinine and Cadmium, as a Mechanism in Smoker Men Infertility

Background Nicotine, cotinine and cadmium are harmful components of cigarettes that have an effect on human reproductive function. Although the effects of cigarette smoke on male reproductive function is characterized in several articles its mechanism of action is still unknown. In the present study, we investigate the effect of nicotine, cotinine and cadmium on human sperm creatine kinase acti...

متن کامل

Kinetic Investigation of Myeloperoxidase upon Interaction with Copper, Cadmium, and Lead Ions

Background: Myeloperoxidase (MPO), which is abundantly expressed in neutrophils, catalyzes the formation of a number of reactive oxidant species. However, evidence has emerged that MPO-derived oxidants contribute to tissue damage and initiation and propagation of inflammatory diseases, particularly, cardiovascular diseases. Therefore, studying the regulatory mechanisms of the enzyme activity is...

متن کامل

Quantum Mechanical Approach for the Catalytic Mechanism of Dinuclear Zinc Metallo-β-lactamase by Penicillin and Cephalexin: Kinetic and Thermodynamic Points of View

Metallo-β-lactamases (MβL) catalyzing the hydrolytic cleavage of the four-membered β-lactam ring in broad spectrum of antibiotics and therefore inactivating the drug; However, the mechanism of these enzymes is still not well understood. Electronic structure and electronic energy of metallo-β-lactamase active center, two inhibitors of this enzyme including penicillin and cephalexin, and differen...

متن کامل

The Mechanism of Chromium Biosorption by Saccharomyces Cerevisiae

The Biosorption property of S. cerevisiae for chromium uptake was investigated in an immobilized cell bioreactor. Saw dust was utilized as the solid bed in the reactor. Adsorption of S. cerevisiae on saw dust obeys a first order reaction kinetic up to 6 hours. The immobilized biomass particles are porous and exist in the new generation of biological adsorbent. Chromium biosorption was studied i...

متن کامل

Kinetics and Isotherm Studies of the Immobilized Lipase on Chitosan Support

The kinetics and isotherm studies of the immobilized lipase and the mechanism of immobilization on chitosan beads and activated chitosan beads with glutaraldehyde were investigated. The effect of glutaraldehyde on porosity of chitosan was evaluated by FESEM analysis. It was observed that the porosity of the carrier which has activated by glutaraldehyde was substantially increased. The validity ...

متن کامل

ELUCIDATION OF pK VALUES FOR ACTIVE SITE OF HORSERADISH PEROXIDASE AND BINDING STUDY OF INTERACTION WITH N-PHENYL BENZHYDROXAMIC ACID USING A SPECIAL DIFFERENCE SPECTROPHOTOMETRIC TECHNIQUE

The binding behavior of a competitive inhibitor, N-phenylbenzhydroxamic acid (BHA) against horseradish peroxidase (HRP) was studied in order to understand and predict the interaction mechanism of hydrogen donors with the enzyme. The dissociation constants of the complexes of HRP-BHA, HRP-donor and HRP-BHA-azide were estimated at specified conditions by difference spectroscopy. The binding s...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Biochemical Society transactions

دوره 8 3  شماره 

صفحات  -

تاریخ انتشار 1980