A Spectroscopic Investigation of Lactate Dehydrogenase Thermal Stability and Its Interaction with Nadh
نویسندگان
چکیده
Fluorescence spectroscopy was used to study some aspects of thermal denaturation of lactate dehydrogenase (LDH) from rabbit muscle, in the absence and presence of urea and NaCl. Thermal denaturation of LDH seems to be one step and a slightly reversible process. The solution pH has an important influence on the LDH thermal denaturation. The interaction of LDH enzyme with NADH ligand was also investigated. The LDH-NADH complex is characterized by a moderate affinity constant and its formation is entropically driven.
منابع مشابه
An immunoglobulin A1 that inhibits lactate dehydrogenase activity, with reversal of inhibition by addition of NADH.
We discovered a patient with low serum lactate dehydrogenase (LD) activity and an abnormal LD isozyme pattern. We analyzed the patient's LD inhibitor using electrophoresis, affinity chromatography, and immunochemical technologies. The LD activity of the patient's serum was inhibited more strongly at 4 degrees C than at 37 degrees C. The decrease of LD activity was more marked in a mixture of th...
متن کاملStudy of the Interaction of Cinnamaldehyde with Alpha-lactalbumin: Spectroscopic and Molecular Docking Investigation
Cinnamaldehyde is an important compound of the cinnamon essential oil, and it is responsible for the most of the health benefits of cinnamon. Enriching foods such as milk with cinnamaldehyde can lead to greater utilization of cinnamaldehyde properties. In this study, we investigated the interaction of cinnamaldehyde with bovine alpha-lactalbumin. Analyzing the spectrum of alpha-lactalbumin in t...
متن کاملInvestigation and Determination the Binding Site of Glycyrrhizin of Liquorice to DNA
Glycyrrhizin(GL), is a triterpenoid saponin found in glychyrrhiza glabra (liquorice). This compound is a frequently used and very effective drug for the treatment of various malignancies. This study was designed to examine the interactions of glycyrrhizin with calf thymus DNA in aqueous solution at physiological conditions. FTIR spectroscopic method was used to determine the ligand binding mode...
متن کاملMeasurement of total lactate dehydrogenase activity.
Lactate dehydrogenase (LD: EC 1.1.1.27) is the most important clinically of several dehydrogenases occurring in human serum. Lactate dehydrogenase is cytoplasmic in its cellular location and in any one tissue is composed of one or two of five possible isoenzymes. While many of its clinical applications involve quantification of one or more specific serum isoenzymes, an estimate of total LD is r...
متن کاملModification of pig heart lactate dehydrogenase with methyl methanethiosulphonate to produce an enzyme with altered catalytic activity.
Methyl methanethiosulphonate was used to produce a modification of the essential thiol group in lactate dehydrogenase which leaves the enzyme catalytically active. Methyl methanethiosulphonate produced a progressive inhibition of enzyme activity, with 2mM-pyruvate and 0.14mM-NADH as substrates, which ceased once the enzyme had lost 70-90% of its activity. In contrast, with 10mM-lactate and 0.4m...
متن کامل