Abstract
This chapter describes the assay method, purification, and properties of triosephosphate isomerase isolated from the chicken and rabbit muscle. Triosephosphate isomerase activity is measured by linking the isomerization reaction to either of the nicotinamide adenine dinucleotide (NAD + )–nicotinamide adenine dinucleotide dehydrogenase (NADH 2 )-dependent enzymic reactions. The D-glyceraldehyde 3-phosphate/α-glycerophosphate dehydrogenase procedure exhibits substrate inhibition at high concentrations of D-glyceraldehyde 3-phosphate, and both triosephosphate isomerase and α-glycerophosphate dehydrogenase are inhibited by phosphate and sulfate ions. In the dihydroxyacetone phosphate/glyceraldehyde- 3-phosphate dehydrogenase procedure, the triosephosphate isomerase is inhibited by arsenate ions, an essential component of the secondary enzyme reaction system. The steps involved in the purification of triosephosphate isomerase from the chicken muscle and rabbit muscle are also discussed in the chapter. Commercial frozen chickens for domestic consumption are used as the source of the enzyme. The initial extraction and ammonium sulfate fractionation are carried out at temperatures below 10°C, but chromatographic procedures are carried out at room temperatures. The structure-function relationships of triosephosphate isomerase from both the chicken and rabbit muscle are examined in the chapter.
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