L7525
L-Lactic Dehydrogenase from porcine heart
ammonium sulfate suspension, ≥200 units/mg protein
Sinônimo(s):
(S)-Lactate: NAD+ oxidoreductase, L-LDH, LAD, LD, Lactate
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About This Item
Produtos recomendados
fonte biológica
Porcine heart
Nível de qualidade
Formulário
ammonium sulfate suspension
atividade específica
≥200 units/mg protein
nº de adesão UniProt
atividade externa
glutamic-oxalacetic transaminase ≤0.1%
malic dehydrogenase, glutamic-pyruvic transaminase and pyruvate kinase ≤0.06%
temperatura de armazenamento
2-8°C
Informações sobre genes
pig ... LDHA(407245)
Descrição geral
Research area: Cell Signaling
Lactic Dehydrogenase (LDH) is a cytoplasmic enzyme encoded by LDHA, LDHB, LDHC, and LDHD genes, and categorized as an oxidoreductase. It is widely distributed throughout the body, particularly in muscle, liver, and kidney. LDH demonstrates five isomeric forms that form tetramers with two types of subunits: muscle (M) and heart (H).
Lactic Dehydrogenase (LDH) is a cytoplasmic enzyme encoded by LDHA, LDHB, LDHC, and LDHD genes, and categorized as an oxidoreductase. It is widely distributed throughout the body, particularly in muscle, liver, and kidney. LDH demonstrates five isomeric forms that form tetramers with two types of subunits: muscle (M) and heart (H).
Aplicação
L-Lactic Dehydrogenase from porcine heart has been used:
- as a component of the reaction buffer to measure the GTPase activity of EngA bound to the bacterial 50S subunit to study its structure and function.
- as a component of the enzyme solutions to test the sensitivity of multiphoton NAD(P)H fluorescence lifetime imaging (FLIM) in key enzymatic steps controlling the path of carbon from glucose uptake to electron transport chain (ETC) activity.
Ações bioquímicas/fisiológicas
Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.
Lactate dehydrogenase (LDH) enzyme is responsible for the conversion of pyruvate to lactate, during glycolysis under hypoxic conditions, while also converting NADH to NAD+. Moreover it acts as a crucial regulator of gluconeogenesis and DNA metabolism. Increased serum LDH levels are detected in conditions such as cancer, HIV infection, muscular dystrophy, megaloblastic anemia, extreme hypothermia, hepatitis, meningitis, hypoxia, etc.
Definição da unidade
One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.
forma física
Suspension in ammonium sulfate and 0.1 M potassium phosphate, pH 7.0
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Resp. Sens. 1
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 1
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
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Joe T Sharick et al.
Scientific reports, 8(1), 5456-5456 (2018-04-05)
While NAD(P)H fluorescence lifetime imaging (FLIM) can detect changes in flux through the TCA cycle and electron transport chain (ETC), it remains unclear whether NAD(P)H FLIM is sensitive to other potential fates of glucose. Glucose carbon can be diverted from
H P Schär et al.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 360(7), 795-807 (1979-07-01)
Lactate dehydrogenases from thermophilic bacilli (Bacillus stearothermophilus, Bacillus caldotenax) and from mesophilic bacilli (Bacillus X1, Bacillus subtilis) have been isolated by a two-step purification procedure. Only one type (LDH-P4) composed of four identical subunits (Mr 34 000 or 36 000)
M J Adams et al.
Proceedings of the National Academy of Sciences of the United States of America, 70(7), 1968-1972 (1973-07-01)
The binding of coenzyme and substrate are considered in relation to the known primary and tertiary structure of lactate dehydrogenase (EC 1.1.1.27). The adenine binds in a hydrophobic crevice, and the two coenzyme phosphates are oriented by interactions with the
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Artigos
Instructions for working with enzymes supplied as ammonium sulfate suspensions
Protocolos
Enzymatic Assay of L-Lactic Dehydrogenase (EC 1.1.1.27)
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