- L-Lactic dehydrogenase
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- $0.00 / 1g
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2025-10-31
- CAS:9001-60-9
- Min. Order: 1g
- Purity: 98.0%
- Supply Ability: 1kg/month
- LACTATE DEHYDROGENASE
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- $5.00 / 1kg
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2025-05-26
- CAS:9001-60-9
- Min. Order: 1kg
- Purity: 0.99
- Supply Ability: 10000
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| | L-Lactic dehydrogenase Basic information |
| | L-Lactic dehydrogenase Chemical Properties |
| storage temp. | 2-8°C | | solubility | aqueous buffer: soluble | | form | suspension | | color | white | | PH | 7.5 | | biological source | rabbit muscle | | Water Solubility | low ionic strength buffer: soluble
water: soluble | | Merck | 13,5349 | | Specific Activity | 800-1,200units/mg protein | | CAS DataBase Reference | 9001-60-9 | | EPA Substance Registry System | Dehydrogenase, lactate (9001-60-9) |
| | L-Lactic dehydrogenase Usage And Synthesis |
| Chemical Properties | Off-white lyophilized powder or crystalline suspension of 3.2 mol/L ammonium sulfate, soluble in water, pI of 4.6, optimum pH 6.0.Stability: crystalline enzyme solution can be stored for 6-8 weeks with unchanged activity, sulfate suspension can be stabilized for more than a year, very dilute solution is unstable; optimum temperature of 39 ℃, rapid inactivation of temperatures above 60 ℃. Inhibitors are excess pyruvate, excess NAD, oxalic acid, oxalic acid monoamide, hydroxymalonic acid, malonic acid, urea, Cu2+, Hg2+, Ag+, 4-chloromercuric benzoic acid, pyrophosphoric acid or phosphate buffer and non-competitive inhibitors formed from coenzyme I (NAD) in alkaline inhibit oxidation reaction, excess lactate and non-competitive inhibitors formed from reduced coenzyme I (NADH) inhibit reduction reaction. inhibitors inhibit the reduction reaction; activators are 2-amino-2-methyl-1-propanol, fluoride, diethanolamine, and heparin (oxidizing). Enzymatic reaction: pyruvate + reduced coenzyme I + H+ ═ lactate + coenzyme I. | | Uses | L-Lactic Dehydrogenase from bovine heart has been used in ATPase assay of R2 complex Rvb1p-Rvb2p, RecA protein and sarcoplasmic reticulum Ca2+-ATPase (SERCA). | | Uses | L-Lactic dehydrogenase is used in the determination of pyruvate (used in conjunction with reduced coenzyme) and in the diagnosis of myocardial infarction and leukemia. | | Uses | L-Lactic Dehydrogenase from bovine heart has been used as a standard in cytotoxicity assay. It has also been used in glutamic pyruvic transaminase (GPT) assay. | | General Description | L-lactate dehydrogenase (LDH) is an enzyme that catalyzes the conversion of lactate to pyruvate.?In particular, lactic dehydrogenase A (LDHA) is mainly found in skeletal muscle, and for that reason is known as the M subunit. This recombinant form of LDHA has a C-terminal histidine-tag.
The gene LDHA (L-lactate dehydrogenase A chain) is mapped to human chromosome 11p15. It is a subunit of lactate dehydrogenase. | | Biochem/physiol Actions | Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids. | | Purification Methods | A forty-fold purification of the dehydrogenase is effected by affinity chromatography using Sepharose 4B coupled to 8-(6-aminohexyl)amino-5'-AMP or -NAD . [Lees et al. Arch Biochem Biophys 163 561 1974, Pesce et al. J Biol Chem 239 1753 1964.] |
| | L-Lactic dehydrogenase Preparation Products And Raw materials |
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