Abstract
Rabbit muscle troponin complex covalently bound to CNBr-activated Sepharose 4B was shown to interact with soluble lactate dehydrogenase with a stoichiometry of 2 mol lactate dehydrogenase/mol of troponin. The presence of Ca 2+ influenced the strength of association (the K D values of 0.73 and 2.3 μM were determined in the presence of 200 μM EGTA or 100 μM Ca 2+, respectively). In the absence of Ca 2+, the affinity of lactate dehydrogenase to troponin was strongly pH-dependent, reaching a maximum in the region of pH 6.0–7.0. No changes of catalytic activity was observed as a result of interaction between lactate dehydrogenase and troponin, the enzyme appeared capable of functioning in the bound form.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - General Subjects
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