An amperometric enzyme electrode tor the analysis of glucose Is described. The electrode uses a substituted ferrlcinlum Ion as a mediator of electron transfer between Immobilized glucose oxidase and a graphite electrode. A linear current response, proportional to the glucose concentration over a range commonly found In diabetic blood samples (1-30 mM), is observed. Data are presented on the Influence of oxygen, pH, and temperature upon the electrode. Results with clinical plasma and whole blood samples show good agreement with a standard method of analysis.

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It is well known that phenylhydrazine induces hemolytic anemia. This is thought to result from the reaction of phenylhydrazine with hemoglobin. The accompanying oxidation of phenylhydrazine leads to the formation of a number of products, including benzene, nitrogen, hydrogen peroxide, superoxide anion and the phenyl radical. The products formed depend critically on the conditions of the experiment, especially the amount of oxygen present. It is now known that oxyhemoglobin and myoglobin react with phenylhydrazine to yield a derivative of hemoglobin containing N-phenylprotoporphyrin in which the heme group is modified. The recent identification of sigma-phenyliron(III) porphyrins in phenylhydrazine-modified metmyoglobin has aided elucidation of the mechanism of hemoglobin modification. Mechanistic schemes are proposed to account for product formation.

The direct electrochemistry of the flavin-containing monooxygenase, pentachlorophenol hydroxylase (PCPH), at an edge plane graphite electrode was observed and a catalytic response, linear with concentration, was found with the substrate pentachlorophenol (PCP).

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