Direkt zum Inhalt
Merck
Alle Fotos(1)

Key Documents

Weitere Dokumente

L5135

Sigma-Aldrich

L-Leucin-Dehydrogenase aus Bacillus cereus

lyophilized powder, ≥60 units/mg protein

Synonym(e):

L-Leucine:NAD+ oxidoreductase (deaminating)

Anmeldenzur Ansicht organisationsspezifischer und vertraglich vereinbarter Preise
Alle Fotos(1)

About This Item

CAS-Nummer:
9082-71-7
EC-Nummer:
1.4.1.9 (BRENDA, IUBMB)
MDL-Nummer:
MFCD00147461
UNSPSC-Code:
12352204
NACRES:
NA.54

Form

lyophilized powder

Qualitätsniveau

200

Spezifische Aktivität

≥60 units/mg protein

Mol-Gew.

245 kDa

Lagertemp.

−20°C

Suchen Sie nach ähnlichen Produkten? Aufrufen Leitfaden zum Produktvergleich

Allgemeine Beschreibung

L-Leucine Dehydrogenase is a member of the amino acid dehydrogenase family.

Anwendung

L-Leucine Dehydrogenase from Bacillus cereus has been used to determine the branched-chain amino acids (BCAA) spectrophotometrically in serum samples.

Biochem./physiol. Wirkung

Leucine Dehydrogenase is a nicotinamide adenine dinucleotide hydrogen (NADH)-dependent oxidoreductase. It is involved in catalyzing the reductive amination of aliphatic 2-oxo-acids to their respective L-amino acids.

Einheitendefinition

One unit will convert 1.0 μmole of L‑leucine to α-ketoisocaproate per min at pH 10.5 at 37 °C.

Sonstige Hinweise

contains lysine

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)

Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

Besitzen Sie dieses Produkt bereits?

In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

K Selber et al.
Journal of chromatography. B, Biomedical sciences and applications, 743(1-2), 21-30 (2000-08-15)
Mathematical strategies were applied to optimise the extraction of recombinant leucine dehydrogenase from E. coli homogenates and endoglucanase 1 from culture filtrates of Trichoderma reesei in polyethylene glycol-phosphate systems. The goal was to test mathematical tools which could facilitate the
M B Ansorge et al.
Applied microbiology and biotechnology, 53(6), 668-673 (2000-08-05)
The established Escherichia coli expression vectors ptrc99a, pKK223-3, pPLlambda, pAsk75, pRA95, and pRA96, which differ in copy number, mode of induction, selection marker, and use of par sequences for stabilization, were investigated for the stable expression of recombinant L-leucine dehydrogenase
S Guangdong et al.
The Journal of antibiotics, 54(1), 66-73 (2001-03-28)
Shengjimycin is a group of 4"-acylated spiramycins with 4"-isovalerylspiramycin as the major component, produced by recombinant S. spiramyceticus F21 harboring a 4"-O-acyltransferase gene from S. mycarofaciens 1748. A stable bioengineered strain of Streptomyces spiramyceticus WSJ-1 was constructed by integrating the
Peng-Hu Zhang et al.
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 23(2), 268-272 (2007-04-28)
The purification and the characteristics of an enzyme from Morganella morganii J-8, which could produce d-pseudoephedrine from 1-phenyl-2-methylamine-acetone, were performed in this study. In this research, first, cells were disrupted by ultrasonic treatment at 4 degrees C. The carbonyl enantioselective
Tatyana A Muranova et al.
Acta crystallographica. Section D, Biological crystallography, 58(Pt 6 Pt 2), 1059-1062 (2002-05-31)
Leucine dehydrogenase is an octameric enzyme which belongs to the superfamily of amino-acid dehydrogenases and catalyses the reversible oxidative deamination of leucine to 2-ketoisocaproate, with the corresponding reduction of the cofactor NAD(+). Catalysis by this enzyme is thought to involve
Alle zugehörigen Dokumente anzeigen

Unser Team von Wissenschaftlern verfügt über Erfahrung in allen Forschungsbereichen einschließlich Life Science, Materialwissenschaften, chemischer Synthese, Chromatographie, Analytik und vielen mehr..

Setzen Sie sich mit dem technischen Dienst in Verbindung.