Altered Kinetics Properties of Erythrocyte Lactate Dehydrogenase in Type II Diabetic Patients and Its Implications for Lactic Acidosis
Autor: | Sunita S Bhise, Aniket V Mali, Mahabaleshwar V. Hegde, Surendra S. Katyare |
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Rok vydání: | 2017 |
Předmět: |
chemistry.chemical_classification
medicine.medical_specialty Pyruvate dehydrogenase kinase biology Clinical Biochemistry 030209 endocrinology & metabolism 030204 cardiovascular system & hematology medicine.disease Enzyme assay 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Enzyme Endocrinology chemistry Biochemistry Lactate dehydrogenase Lactic acidosis Internal medicine Diabetes mellitus medicine biology.protein Original Article Glycolysis Enzyme kinetics |
Zdroj: | Indian Journal of Clinical Biochemistry. 33:38-45 |
ISSN: | 0974-0422 0970-1915 |
DOI: | 10.1007/s12291-017-0637-6 |
Popis: | Recent studies have been noted that the erythrocytes from Type II diabetic patients show significantly altered structural and functional characteristics along with the changed intracellular concentrations of glycolytic intermediates. More recent studies from our laboratory have shown that the activities of enzymes of glycolytic pathway changed significantly in RBCs from Type II diabetic patients. In particular the levels of lactate dehydrogenase (LDH) increased significantly. Lactic acidosis is an established feature of diabetes and LDH plays a crucial role in conversion of pyruvate to lactate and reportedly, the levels of lactate are significantly high which is consistent with our observation on increased levels of LDH. Owing to this background, we examined the role of erythrocyte LDH in lactic acidosis by studying its kinetics properties in Type II diabetic patients. Km, Vmax and apparent catalytic efficiency were determined using pyruvate and NADH as the substrates. With pyruvate as the substrate the Km values were comparable but Vmax increased significantly in the diabetic group. With NADH as the substrate the enzyme activity of the diabetic group resolved in two components as against a single component in the controls. The Apparent Kcat and Kcat/Km values for pyruvate increased in the diabetic group. The Ki for pyruvate increased by two fold for the enzyme from diabetic group with a marginal decrease in Ki for NADH. The observed changes in catalytic attributes are conducive to enable the enzyme to carry the reaction in forward direction towards conversion of pyruvate to lactate leading to lactic acidosis. |
Databáze: | OpenAIRE |
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