The effect of hydrogen peroxide on the rate of oxygen consumption of frog skin

✍ Scribed by Carlson, Loren D. ;Marsh, Gordon

• Publisher: Wiley (John Wiley & Sons)
• Year: 1943
• Tongue: English
• Weight: 915 KB
• Volume: 22
• Category: Article
• ISSN: 0095-9898
• DOI: 10.1002/jcp.1030220202

✦ Synopsis

Hydrogen peroxide in oxygenated Ringer's solution increases the steady E.N.F. of frog skin from a just detectable amount at 1.5 x 10-6M peroxide to a maximum at,8 X lo-* 31 (Marsh and Carlson, '41).

Higher concentrations reversibly depress the steady potential difference below the control level. This behavior conforms precisely to the expectation from Lund 's oxidation-reduction theory of bioelectric potentials and is not readily predictable upon any other grounds. I t follows from the formulation of cellular E.M.F. (Marsh, '35) that hydrogen peroxide must function in the metabolism of the skin as an oxidizing agent which is consumed a t a rate proportional to its available concentration.

Relatively little is known of the role of peroxide in the normal mettabolism of tissues (c. g., Holmes, '37, p. 61). Although its toxicity and its effect upon other physiological processes has been determined (e. g., hlaclcod, '42), but one instance has been found where the inflnence of added peroxide on the respiratory exchange has been measured. Addition of .004 M peroxide inhibits oxygen uptake of Acetobacter peroxydans (which lacks peroxidase), but .00125 M peroxide produces an acceleration ( Qo, =.500) (Wieland and Pistor, '36).

Hydrogen peroxide is known to be formed in vitro as an end product of oxidation by many enzyme systems: among them xanthine oxidase, tyramine oxidase, amino acid oxidase, uricase and the yellow ferments (Oppenheimer and Stern, '39, pp. 2 2 4 4 ; Green, '40). In vivo it commonly cannot be detected because it is decomposed or, more probably, consumed as rapidly as formed. Production in amounts analytically demonstrable has been reported only for cultures of streptococci, pneumococci and lactic acid bacteria, all of which lack iron-porphyrin enzyme systems (Oppenheimer and Stern, loc. cit.).