Description
Native Porcine Lactate Dehydrogenase
| Catalog number: | B2017346 |
| Lot number: | Batch Dependent |
| Expiration Date: | Batch dependent |
| Amount: | 100 KU |
| Molecular Weight or Concentration: | ~136.7 kDa |
| Supplied as: | Powder |
| Applications: | a molecular tool for various biochemical applications |
| Storage: | 20C |
| Keywords: | LAD, LD, L-LDH, (S)-Lactate, NAD+ oxidoreductase |
| Grade: | Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity>18 M-cm) and are filtered through 0.22 um. |
References
- Pfleiderer G, Nagel G, Bhler H. Limited proteolysis of lactate dehydrogenase from porcine heart with trypsin: characterization and reactivation of the fragments Experientia. 1991 May 15;47(5):470-5.
- Opitz U, Rudolph R, Jaenicke R, Ericsson L, Neurath H. Proteolytic dimers of porcine muscle lactate dehydrogenase: characterization, folding, and reconstitution of the truncated and nicked polypeptide chain Biochemistry. 1987 Mar 10;26(5):1399-406.
- Zheng YB, Meng FG, Chen BY, Wang XC. Inactivation and conformational changes of lactate dehydrogenase from porcine heart in sodium dodecyl sulfate solutions Int J Biol Macromol. 2002 Dec 20;31(1-3):97-102.
- Chilson OP, Chilson AE. Perturbation of folding and reassociation of lactate dehydrogenase by proline and trimethylamine oxide Eur J Biochem. 2003 Dec;270(24):4823-34.
- Jeckel D, Anders R, Pfleiderer G. [Kinetics of trypsin digestion of native lactate dehydrogenase from the porcine myocardium] Hoppe Seylers Z Physiol Chem. 1972 May;353(5):719.
- Girg R, Rudolph R, Jaenicke R. Limited proteolysis of porcine-muscle lactic dehydrogenase by thermolysin during reconstitution yields dimers Eur J Biochem. 1981 Oct;119(2):301-5.
- Fernandes S, Hatti-Kaul R, Mattiasson B. Selective recovery of lactate dehydrogenase using affinity foam Biotechnol Bioeng. 2002 Aug 20;79(4):472-80.
- Girg R, Jaenicke R, Rudolph R. Dimers of porcine skeletal muscle lactate dehydrogenase produced by limited proteolysis during reassociation are enzymatically active in the presence of stabilizing salt Biochem Int. 1983 Oct;7(4):433-41.
- Grebenshchikova OG, Andrianova LE, Prozorovski VN. [Antigenic activity of porcine muscle lactate dehydrogenase fragment 180-214 containing the histidine residue of the isoenzyme active center] Biokhimiia. 1989 Mar;54(3):361-9.
