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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-617-8
MDL number:
Specific activity:
800-1,200 units/mg protein
type
Type II
form
ammonium sulfate suspension
specific activity
800-1,200 units/mg protein
mol wt
140 kDa
foreign activity
pyruvate kinase, myokinase, malic dehydrogenase, glutamic-pyruvic transaminase, glutamic-oxalacetic transaminase and α-glycerophosphate dehydrogenase ≤0.01%
shipped in
wet ice
storage temp.
2-8°C
Quality Level
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Application
L-Lactic Dehydrogenase from rabbit muscle has been used:
- for protein-binding measurement
- to detect the action of oxaloacetate decarboxylase
- to determine serum L- and D-lactate
Biochem/physiol Actions
Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.
Lactic dehydrogenase is responsible for the conversion of pyruvate to lactate in the fermentative metabolism.
Analysis Note
Protein determined by biuret.
General description
Lactic Dehydrogenase (LDH) has a total molecular weight of 140 kDa and is composed of 4 subunits which are designated M subunit (muscle) and H subunit (heart). These subunits may be mixed in any of 5 combinations (M4, M3H1, M2H2, MH3, and H4). Skeletal muscle contains LDH that is predominately M4 with some small amounts of M3H and traces of H2H2. The H and M subunits are quite similar in molecular weight, but differ substantially in amino acid composition. Rabbit muscle LDH dissociates into dimeric species (MW = ~70 kDa) in acetate-chloride at pH 5.0, the dissociation is reversible. Biochemistry, 13, 3527-3531 (1974). Oxidizes glyoxylate and lactate.
Isoelectric point: 8.4-8.6
Optimal pH : 7.5 .
Isoelectric point: 8.4-8.6
Optimal pH : 7.5 .
Other Notes
One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.
Physical form
Crystalline suspension in 3.2 M (NH4)2SO4 solution, pH 6.0
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk
WGK 1
ppe
Eyeshields, Gloves, type N95 (US)
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