Polarography of proteins

Homolka, Jiri, Polarography of Proteins, Analytical Principles and... 

J. Homolka, Polarography of Proteins and its Chemical Applications (In Czech) (Statni Zdravotnicke Nakladatelstvi, Praha, 1964) p. 143. 

H20. Homolka, J., Polarography of proteins, analytical principles, and applications in biological and clinical chemistry. Methods Biochem. Anal. 19, 435-555 (1971). 

I. D. Ivanov, Polarography of Proteins, Enzymes, and Amino Acids, USSR Academy of Sciences Publishing House, Moscow (1961). In Russian. 

Figure 2. Polarography of protein in Co solution. Left to right) reduction waves of cobalt, protein wave, presodium wave (slightly indicated at the upper margin of the polarogram) polarogram of the Co solution per se, cobalt maximum, and diffusion current of cobalt.

Polarography of Proteins, Analytical Principles and Applications in Biological and Clinical Chemistry. By Jifi HomoUea, Department of Clinical Biochemistry of the Faculty of Medicine, Charles University, Prague, Czechoslovakia. 435... 

Refs. [i] Brdicka R (1933) Coll Czech Chem Common 5 112 [ii] Brdicka R (1937) Nature 139 1020 [Hi] Brdilka R (1947) Research 1 25 [iv[ Brdicka R, Bfezina M, Kalous V (1965) Talanta 12 1149 [v] Muller OH (1963) Polarographic analysis of proteins, amino acids and other compounds by means of Brdicka reaction. In Click D (ed) Methods of biochemical analysis, vol. 11. Interscience, New York, pp 329-403 [vi[ Homolka / (1971) Polarography of proteins, analytical principles and applications in biological and clinical chemistry. In Click D (ed) Methods in biochemical analysis, vol. 19. Wiley, New York, pp 436-555 [vii] Hart IP (1990) Electroanalysis of biologically important compounds. Ellis Horwood, New York, p 92 [viii] Brabec V, Vetterl Y, Vrana O (1996) Electroanalysis of biomacromolecules. In Brabec Y, WalzD, Milazzo C (eds) Techniques in bioelectrochemistry, vol. 3. Birkhduser Yerlag Basel, p 287 [ix] Luo D, Lan ], Zhou C, Luo C (2003) Anal Chem 75 6346 [x] Brdicka R (1942) Z Elektrochem 48 278 [xi] Brdicka R, Wiesner K (1947) Coll Czech Chem Common... 

A variety of physical methods has been used to ascertain whether or not surface ruthenation alters the structure of a protein. UV-vis, CD, EPR, and resonance Raman spectroscopies have demonstrated that myoglobin [14, 18], cytochrome c [5, 16, 19, 21], and azurin [13] are not perturbed structurally by the attachment of a ruthenium complex to a surface histidine. The reduction potential of the metal redox center of a protein and its temperature dependence are indicators of protein structure as well. Cyclic voltammetry [5, 13], differential pulse polarography [14,21], and spectroelectrochemistry [12,14,22] are commonly used for the determination of the ruthenium and protein redox center potentials in modified proteins. 

Electrochemistry finds wide application. In addition to industrial electrolytic processes, electroplating, and the manufacture and use of batteries already mentioned, the principles of electrochemistry are used in chemical analysis, e.g.. polarography, and electrometric or conductometric titrations in chemical synthesis, e.g., dyestuffs, fertilizers, plastics, insecticides in biolugy and medicine, e g., electrophoretic separation of proteins, membrane potentials in metallurgy, e.g.. corrosion prevention, eleclrorefining and in electricity, e.g., electrolytic rectifiers, electrolytic capacitors. 

Many applications of polarography in the determination of proteins or simple sulphydryl or disulphide compounds in various biological materials have been described [3]. 

For the estimation of traces of proteins in nucleic acid preparations, a pulse polarographic method is more suitable than classical polarography... 

The development of the electrochemistry of biopolymers has paralleled research on their structures. In the case of proteins the basic research by the polarography school of Heyrovsky and the electrophoresis school of Tiselius and Theorell started in the thirties, whereas research on nucleic acids and polysaccharides was the focus of interest about 20 years later at Jena and Brno. The study of the behavior of proteins and nucleic acids as polyelectrolytes in solution is now a very broad field and the main topics of research are... 

The history of the use of electrochemical methods to study the properties of proteins, enzymes, and their component structural units is several decades old. Until quite recently, these studies were primarily associated with the use of polarography to solve analytical problems. The polarographic method of analysis has become very popular for determination of proteins, enzymes, and nucleic acids.It has been found that proteins irreversibly adsorb on mercury and in the presence of cobalt salts promote the evolution of hydrogen. In this case wave height is proportional to the amount of adsorbed protein. These studies have been summarized in some reviews and monographs. " "" ... 

We bring proofs that pathological proteins have a different quality, whieh is discernible by polarography and is manifested by a smaller increase in the wave height after denaturation by alkali hydroxide in albumin, and by a diminished elution from the paper into the solution after addition of alkali hydroxide in globulins. In globulin fractions, the nature of proteins is typically changed above all at the very places where... 

ABSTRACT. After a brief survey of the different types of natural copper proteins, and their metal-centred main functions, the characteristics of "good" synthetic models are outlined. Electrochemical studies, by cyclic voltammetry and/or differential pulse polarography, of some representative models are overviewed. Recent, unpublished, results on several copper complexes intended to mimick the Type I copper sites are described and briefly discussed. 

Very recently, the differential pulse polarography of some copper proteins, made possible by promotion, was studied and discussed by Kova et. al. [12]. 

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