Comparative Study on the Conformational Mobility of Muscle Lactate Dehydrogenase from Loach Fish Adapted to Different Temperatures Using Differential Scanning Microcalorimetry
نویسندگان
چکیده
Differential scanning microcalorimetry was used to assess the conformational stability of muscle lactate dehydrogenase (M4-LDH) from skeletal muscle of Misgurnus fossilis (loach) fishes adapted to low (the “cold” enzyme) and high (the “warm” enzyme) environmental temperatures. It was found that the denaturation temperature Td was the same for both forms of lactate dehydrogenase, whereas the denaturation enthalpy ∆H of the “warm” enzyme was higher at all pH values studied. For the operating pH values, three stages of lactate dehydrogenase denaturation were found. These results agree with the X-ray data obtained for the dogfish muscle. The main difference between the “warm” and the “cold” enzyme forms is exhibited mostly at the first stage.
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