ELECTROPHORETIC CHARACTERIZATION OF HUMAN DEHYDROGENASES

1965 ◽  
Vol 43 (10) ◽  
pp. 1653-1659 ◽  
Author(s):  
A. M. Katz ◽  
W. Kalow

Several isoenzymes of lactate, malate, and isocitrate dehydrogenases have been demonstrated in human skeletal muscle, heart, and liver. Single zones of activity were shown for glucose-6-phosphate and glutamate dehydrogenases. A zone possessing a marked reducing capacity towards nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate was visualized in the absence of any substrate, using the tetrazolium-coupled histochemical method. This zone represents the so-called "nothing dehydrogenase".

1977 ◽  
Vol 23 (9) ◽  
pp. 1293-1298 ◽  
Author(s):  
Kalemani Mulongoy ◽  
Gerald H. Elkan

A nicotinamide adenine dinucleotide (NAD) linked 6-phosphogluconate (6-PG) dehydrogenase has been detected in Rhizobium. The enzyme activity is similar in both slow- and fast-growing rhizobia. The nicotinamide adenine dinucleotide phosphate (NADP) dependent 6-PG dehydrogenase was detected only in the fast growers and was more than twice as active as the NAD-linked enzyme. Partial characterization of the products of 6-PG oxidation in Rhizobium suggests that the NADP-linked enzyme is the decarboxylating enzyme of the pentose phosphate (PP) pathway (EC 1.1.1.44) whereas a phosphorylated six-carbon compound, containing ketonic group(s), is the product of the oxidation catalyzed by the NAD-linked enzyme.


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