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일반 설명
Malic Dehydrogenase is a ubiquitous enzyme, which exists in two isoforms in eukaryotic cells.
Malic dehydrogenase exists as a dimer with each subunit containing an NAD-binding domain and a substrate-binding carboxy-terminal domain required for activity.
Malic dehydrogenase is a cytoplasmic isozyme and an important catalyst in the tricarboxylic acid cycle.
애플리케이션
Malic Dehydrogenase from porcine heart has been used:
- in qualitative protein binding measurements
- to test internally calibrated electrochemical continuous enzyme assay (ICECEA) with model enzyme pair
- to investigate the effect of chaperone on the refolding of heat-denatured malate dehydrogenase
Malic dehydrogenase has been used in a study to assess the effect of an immunomodulator S2 complex on the enzymes of the parasites. It has also been used in a study to investigate the heterogeneity of lactic and malic dehydrogenase in cerebrospinal fluid.
생화학적/생리학적 작용
Malic Dehydrogenase (MDH) plays an important role in the citric acid cycle in mitochondria. It catalyzes the interconversion of substrates malate and oxaloacetate with the simultaneous oxidation/reduction of NAD/NADH+. MDH present in the cytosol is involved in the shuttling of malate/aspartate.
단위 정의
One unit will convert 1.0 μmole of oxalacetate and β-NADH to L-malate and β-NAD per min at pH 7.5 at 25°C.
물리적 형태
Suspension in 2.8 M (NH4)2SO4 solution, pH 6.0
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
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시험 성적서(COA)
Lot/Batch Number
이미 열람한 고객
Electrochemical Coupled-Enzyme Assays at Carbon Nanotubes
Zhang M, et al.
Analytical Chemistry, 86(18), 9330-9334 (2014)
Heterogeneity of lactic and malic dehydrogenase in cerebrospinal fluid
Lowenthal, A., et al.
Journal of Neurochemistry, 7, 135-140 (2006)
Sensing NADH conformation using phasor analysis on fluorescence spectra
Palo D, et al.
Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 186(3), 105-111 (2017)
Malate dehydrogenases-structure and function
Minarik P, et al.
General Physiology and Biophysics, 21(3), 257-266 (2002)
Sandip K Nandi et al.
Biochemical and biophysical research communications, 533(4), 1352-1358 (2020-10-22)
The chaperone activity of α-crystallin is important for maintaining the transparency of the human lens. αB-crystallin (αBC) is a long-lived protein in the lens that accumulates chemical modifications during aging. The formation of advanced glycation end products (AGEs) through glycation
문서
Instructions for working with enzymes supplied as ammonium sulfate suspensions
프로토콜
Spectrophotometric assay evaluates malic dehydrogenase activity using bovine heart enzyme with critical histidine residue at active site.
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