the lactate dehydrogenase


Enzymes are protein molecules which catalyst the biological reactions within populating systems [ 23 ] . They provide a reaction surface to which a substrate can easy adhere and a suited environment for the reaction to happen. They bring the reactants together and point them in such a manner that they attain their transition-state constellations. They weaken the high-energy bonds in the reactants, so that the reaction can happen fast and give a merchandise which is so released [ 8 ] . Sometimes, the enzymes may besides take part in the mechanism of reaction but remain unchanged at the terminal of the reaction [ 6, 18 ] .

An enzyme catalyzed reaction is a reversible reaction which means that the reaction can happen in both the waies. Therefore an enzyme can be defined as an agent that speeds up the attack to equilibrium with the starting stuffs and merchandises being unaffected [ 8 ] .

One of the most of import and basic map of an enzyme is to increase the velocity of the reaction they catalyze [ 6, 18 ] . This is done by take downing the activation energy, which is the energy difference between the get downing stuff and the passage province, and it is the size of this activation energy that determines the rate of a reaction [ 8 ] .

“ Most cellular reactions occur about a million times faster than they would in the absence of an enzyme ” [ 6 ] .

Enzymes function with high specificity for merely one reactant and catalyse the specific reactions compared to most chemical accelerators which catalyze a broad scope of reactions. The enzyme contains an active site which is the country with an appropriate form and functional groups to let the reactant or substrate to adhere to the enzyme. The binding can sooner be inhibited by the enzyme with the aid of inhibitor. An enzyme besides contains a non-protein portion called cofactors [ 8 ] . The cofactor may be a either

  • An organic group called prosthetic group which binds for good to enzyme [ 8 ]
  • Positively charged metal ions called activators which bind temporarily to enzyme [ 8 ]
  • Organic molecules called coenzymes which are derived from protein and adhere temporarily to enzyme-substrate complex [ 8 ] .

Each cell in the life system contains a alone set of some 3000 enzymes and each enzyme is every bit of import to the cell. Enzymes have greatly been studied by insulating them from cell and do them work in a trial tubing environment [ 23 ] .

Lactate dehydrogenase:

“ Lactate dehydrogenase ( LDH ) is an enzyme nowadays in a broad assortment of beings, including workss and animate beings ” . [ 23 ] Its Enzyme Comission figure is EC [ 23 ] where ;

EC 1 = oxidoreductase

EC 1.1 = moving on the CH-OH group of the giver

EC 1.1.1 = With NAD or NADP as acceptor

EC = L-lactate dehydrogenase [ 23 ]

Therefore, it is an oxidoreductase enzyme that catalyzes the interconversion of pyruvate and lactate accompanied by the interconversion of NADH and NAD+ [ 2, 5, 7, 12, 14 ] . The reaction is as following:

During anaerobiotic glycolysis ( limited or no O during intense muscular activity ) , the enzyme converts pyruvate to breastfeed [ 24 ] . The contrary reaction occurs in liver due to feedback suppression when the lactate concentration is high [ 24 ] . Such a rhythm is called Cori rhythm which was discovered by Carl Cori and Gerty Cori and the rhythm [ 24 ] is shown below:

LDH is non specific to any individual tissue and is found in many tissues particularly the bosom, liver, kidney, skeletal musculus, encephalon, blood cells, and lungs [ 23 ] .

Kinetic Properties:

Kinetic surveies indicate that lactate binds to substrate and co-enzyme in the undermentioned order [ 14 ] :

The binding order is discussed in item under the subdivision ‘LDH Catalytic Cycle ‘ .

LDH Beginning:

LDH is available in most workss and animate beings [ 23 ] . Commercially available LDH is chiefly extracted from the undermentioned beginnings:

  • Chicken or Meleagris gallopavo ( besides recombinant and lyophilized )
  • Bovine bosom ( besides lyophilized )
  • Rabbit musculus ( besides recombinant )
  • Porcine bosom and musculus ( besides lyophilized )
  • Human bosom and red blood cell ( besides lyophilized ) [ 23 ]

For the research lab uses, LDH can easy be purified by consecutive ammonium sulphate precipitations.

LDH Structure:

LDH is present in the signifier of its isozymes ( besides called isoenzymes ) which are tetramers [ 12 & A ; 22 ] . Each tetramer consists of four sub-units or monomers each with mass of 36 kDa giving the tetramer the mass of 144 kDa [ 12 ] . Each monomer consists of a peptide concatenation of 334 aminic acids with its ain active centre [ 12 ] . The undermentioned figure shows a high-ranking construction of tetramer ( A-1 ) and detail construction of the active centre of one of its monomer ( A-2 )

It is clear from the above figure ( A-1 ) that the fractional monetary units occupy equal places in a tetramer. In the figure ( A-2 ) shows the peptide anchor, substrate ( lactate ) , the co-enzyme ( NAD+ ) and the three amino acerb side ironss ( Arg-109, Arg-171 and His-195 ) and peptide cringle formed by amino acid residues 98-111 [ 12 ] . In the absence of lactate and NAD+ , the active Centre is unfastened and entree to substrate binding site is allowed [ 12 ] . In the presence of lactate NAD+ composites as shown in the figure, the active centre is closed by peptide cringle and no entree is allowed to the binding site [ 12 ] .

The LDH isozymes are made up of two distinguishable fractional monetary units – M and H, holding different amino acid sequences which make them different in footings of catalytic belongingss [ 12 ] . The undermentioned figure shows subdivisions from amino acid sequences of M and H cistrons.

The amino acerb sequence of M and H cistrons [ 12 ] .

“ The differences in sequence between the M and H fractional monetary units are chiefly conservative-i. e. , both residues are of the same type, e. g. Glycine ( G ) and alanine ( A ) , or arginine ( R ) and lysine ( K ) . Non-conservative exchanges are less frequent-e. g. , lysine ( K ) for glutamine ( Q ) , or threonine ( T ) for glutamic acid ( E ) ” [ 12 ] . The H cistron is more strongly negatively charged than M cistron due to higher figure of acidic residues [ 12, 14 ] . This can be observed in cataphoresis where LDH-1 incorporating four H units move faster than other isozymes while the LDH-5 which contains 4 M fractional monetary units is the slowest [ 5, 12 & A ; 14 ] .

LDH Catalytic Cycle:

The figure shows that nicotinamide adenosine dinucleotide ( NAD+ ) acts as a coenzyme for LDH that helps the enzyme to catalyse the dehydrogenation of lactic acid ( lactate ) to pyruvic acid ( pyruvate ) . NAD+ binds to active site of the enzyme along with lactic acid and acts as an oxidizing agent. It is converted to its reduced signifier ( NADH ) at the terminal of the reaction. On the other manus, NADH acts as a reduction agent and binds to the enzyme and a rearward reaction occurs [ 8 ] .

The overall consequence of LDH is that it catalyzes the transportation of hydride ions from lactic acid to NAD+ or from NADH to Pyruvate. LDH does non impact the equilibrium while catalyzing the reaction in either way [ 12 ] . Since LDH catalyses the reaction in both way, the catalytic procedure can be represented as a closed cringle [ 12 ] . Koolman et Al. has shown the rhythm utilizing six snapshots while depicting the stairss really abruptly lived doing them hard to observe [ 12 ] . The six stairss are shown in the undermentioned figure.

The figure shows the three amino acid residues: arginine-171, histidine-195 and arginine-109, which play an of import function in catalytic rhythm. Other aminic acid residues besides play of import function either straight in the one of the stairss in the catalytic rhythm or indirectly by interceding the binding of the substrate and coenzyme [ 12 ] . “ The positively charged guanidinium group of arginine-171 binds the carboxylate group of the substrate by electrostatic interaction. The imidazole group of histidine-195 is involved in acid-base contact action, and the side concatenation of arginine-109 is of import for the stabilisation of the passage province ” [ 12 ] . The positively charged Arg-171 and Arg-109 do non alter their charge during the contact action while His-195 changes its charge [ 12 ] . The peptide loop dwelling of amino acid residues 98-111 besides plays of import function during the contact action [ 12 ] . It closes the active site after the substrate ( substrate ) binds to the coenzyme ( NAD+ ) in order to except the H2O molecules mostly during the negatron transportation [ 12 ] .

LDH catalystic rhythm.

The six stairss are described as follows.

  1. The first measure shows the free enzyme. The enzyme is without substrate-coenzyme binding and therefore the active site is unfastened [ 12 ] . His-195 is positively charged and is hence represented as E.H+ [ 12 ] .
  2. In measure 2, the coenzyme NADH bounds first [ 12 ] .
  3. Pyruvate binds to the LDH. “ It is of import that the carbonyl group of the pyruvate in the enzyme and the active site in the nicotinamide ring of the coenzyme should hold a reasonably optimum place in relation to each other, and that this orientation should go fixed ( propinquity and orientation of the substrates ) ” [ 12 ] . At this point, the active Centre is closed by peptide cringle [ 12 ]
  4. This is the passage province where oxidation-reduction reaction occurs [ 12 ] . The NADH looses one hydride H- ion which is transferred to the carbonyl C [ 12 ] . “ The transient-and energetically unfavorable -negative charge on the O that occurs here is stabilized by electrostatic interaction with Arg-109 ( stabilisation of the passage province ) ” [ 12 ] . The O atom receives a proton released by His-195 [ 12 ] .
  5. Lactate is bound.
  6. NAD+ is bound. The peptide cringle opens the active Centre and lactate is disassociated from the enzyme [ 12 ] . “ Finally, the oxidised coenzyme NAD+ is released, and initial province ( 1 ) is restored ” [ 12 ]

The same stairss occur in the opposite way during the oxidization of lactate to pyruvate [ 12 ] . The concentration of all the reactants and the pH value determines the way in which the reaction takes topographic point [ 12 ] .

LDH Isozymes:

In mammals, LDH is composed of three fractional monetary units or cistrons: H ( bosom ) and M ( musculus ) [ 5, 12 & A ; 21 ] . LDH is a tetramer of H and M fractional monetary units which means five different combinations of these two fractional monetary units, called isozymes are possible [ 5, 12 & A ; 21 ] . The isozymes differ in catalytic, physical and immunological belongingss [ 5, 12 & A ; 21 ] The H fractional monetary unit is more negatively charged than M fractional monetary unit which makes the isozyme ( HHHH ) move faster towards anode than the other isozymes and appear foremost on the gel [ 5, 12 & A ; 21 ] . Therefore these isozymes are named harmonizing to their electrophoric mobility in the gel with the faster being LDH-1 and the slowest LDH-5 [ 12 & A ; 16 ] .

  • LDH1: This is composed of four H fractional monetary units ( HHHH ) . Largely found in bosom.
  • LDH2: This is composed of three H fractional monetary units and one M fractional monetary unit ( HHHM ) . LDH2, LDH3 and LDH4 are found in all tissues.
  • LDH3: This is composed of two H and two M fractional monetary units ( HHMM ) .
  • LDH4: This is composed of one H and three M fractional monetary units ( HMMM ) .
  • LDH5: This is composed of four M fractional monetary units ( MMMM ) and is found in skeletal musculus in all species and the liver in Equus caballuss and little animate beings.

LDH Isoenzymes

The isozymes have different Km values for pyruvate and therefore are better suited for different environments inside the organic structure. A pure tetramer of M fractional monetary unit i.e. M4, has lower Km for pyruvate and is concentrated in skeleton musculuss which are anaerobiotic [ 5 & A ; 21 ] . Therefore M4 promotes glycolysis by catalysing the production of lactate from pyruvate rapidly and expeditiously [ 14 ] . On the other manus pure tetramer of H fractional monetary unit i.e. H4, has greater Km for pyruvate and is more concentrated in bosom musculuss which is aerophilic [ 14 & A ; 21 ] . Since bosom is non anaerobiotic, it is non necessary to turn the pyruvate into lactate [ 5, 14 ] . Therefore the enzymatic activity of H fractional monetary unit is restrained by pyruvate and other compounds in the bosom structurally similar to the pyruvate [ 14 ] . This pyruvate in bosom can so be used in glycolysis to bring forth ATP for the bosom musculus [ 14 ] .

As said before, H fractional monetary unit predominates the bosom while the M fractional monetary unit predominates the musculus [ 13 ] . As an illustration, the rat bosom contains 78 % of H fractional monetary unit while the legs have merely 11 % of this fractional monetary unit and alternatively hold greater figure of M fractional monetary unit.

In 1962, some research workers investigated the stria forms of LDH isozymes in different animate beings and found that same isozymes of different animate beings have different cataphoretic mobility [ 5 ] . The consequence of their survey is shown below:

In this instance, the sera were all started at the centre line, and sets would migrate either to the positive or negative electrode. They noticed that HHHH migrated the most strongly to the positive electrode and MMMM moved to the negative electrode [ 5 ] .

LDH isozymes separation techniques:

There are a figure of techniques used to divide and assay the LDH isozymes. One of the most effectual techniques is the separation utilizing cellulose ethanoate as separation medium [ 5 ] . Gel based cataphoresis separation techniques are besides used [ 5 ] . Gels used for separation in such techniques include agar gels, amylum and polyacrylamide gel [ 5 ] . Isoelectric concentrating in acrylamide has besides been used [ 5 ] . However, beside their utility for LDH isozyme separation, cataphoresis techniques have several disadvantages [ 5 ] . The following tabular array shows the distribution of LDH enzymes in human tissues and serum utilizing different separation techniques.

“ Different distributions are given by different cataphoretic media in the same tissue, and surveies on the same tissue by different workers utilizing the same medium frequently reveals disagreement ” [ 5 ] . Artefactual bands on the gel looking in the absence of substrate are considered to be doing this [ 5 ] . These sets are caused by due to the reaction between intoxicant dehydrogenase and hints of ethanol nowadays in the reagent [ 5 ] .

This has besides been attributed to the action of LDH on hints of hydroxy-acids found in gel media [ 5 ] . “ Other beginnings of concern include the broad scope of reaction conditions used by assorted writers for transporting out the visual image process and which in many cases are far from optimum ” [ 5 ] . Furthermore, the cataphoretic techniques are non best suited for a big throughput in everyday research labs. To get the better of the issues associating to these techniques, other techniques were developed to use the chemical belongingss of isoenzymes alternatively of cataphoretic belongingss [ 5 ] .

For this intent, chemical and physical differences between the pure tetrameric signifiers, LD1 and LDs were successfully exploited [ 5 & A ; 12 ] . Initial techniques employed trichloromethane and propanone to demobilize all fractions except LD1 but required centrifugation to take denaturized protein prior to transporting out the check which posed an incommodiousness [ 5 ] . Oxalate and Oxamate were besides utilised which inhibit LD1 more than LD5 with Oxamate suppressing human bosom infusion ( LD1 ) by 50 % and human liver infusion ( LD5 ) by merely 20 % [ 5 ] . Neither inhibitor is sufficiently specific to supply distinct diagnostic favoritism [ 5 ] . On the other manus, carbamide is seen as more powerful reagent suppressing LD5 more strongly than LD1 [ 5 ] .

LDH Applications

LDH is an of import enzyme and has found assorted applications in clinical biochemistry, pharmaceuticals, nanotoxicology etc. Some of the applications of LDH are as followers:

LDH in clinical biochemistry:

LDH can function as a great marker for assorted diseases and cell jobs [ 2, 5, 12 & A ; 20 ] . LDH resides inside the cell and ne’er gets into the blood in a healthy cell. When a cell amendss LDH finds its manner into the blood. This elevates the degree of LDH in the blood which can be measured and considered as a general index of the being and badness of ague or chronic tissue harm [ 5 & A ; 20 ] . LDH degree in blood can besides be measured on a regular basis to supervise the intervention advancement. LDH degree can be measured either as entire LDH or LDH isozyme. Entire LDH degree is a general marker of the tissue harm and does non give any indicant of the cause or location of tissue harm [ 5, 12 & A ; 20 ] .

Since LDH isozymes are present in assorted tissues at different degrees, their elevated degrees are helpful in placing the exact nature or cause of the tissue harm and location of the damaged tissue and organ [ 5, 12 & A ; 20 ] . “ For illustration, the liver and skeletal musculuss chiefly produce M fractional monetary units of lactate dehydrogenase ( M for musculus ) , while the encephalon and cardiac musculus chiefly express H fractional monetary units ( H for bosom ) . In effect, each organ has a characteristic isozyme form. Following cardiac infarction, for illustration, there is a strong addition in the sum of LDH-1 in the blood, while the concentration of LDH-5 hardly alterations ” [ 12 ] . Lactate dehydrogenase isoenzyme 1 ( LD-1 ) is used as a tumour marker of source cell tumours [ 4 ] .

Since LDH is present in many tissues, it is really utile in naming tissue amendss and assorted diseases [ 5 & A ; 20 ] . There are a broad assortment of conditions in which LDH degree is elevated. Some of these conditions include myocardial and pneumonic infarction, megaloblasic anaemia, extended carcinomatois, terrible daze and hypoxia, granulocytic or acute anaemia, haemolytic anaemia, infective glandular fever, progressive muscular dystrophy, hepatitis, cirrhosis, clogging icterus, and in craze tremens [ 5 & A ; 20 ] .

LDH obtained from Lactobacillus strains, has been employed for the stereospecific decrease of pyruvate to D-lactate and phenylpyruvate to D-phenyllactate [ 9 ] .

LDH in Industries:

LDH has late been found to be really utile in industrial production of lactate which is widely used in industrial applications such as chemical production. Colombi et Al. and Branduardi et Al. showed the effectivity of LDH in footings of efficiency and economic sciences to bring forth big sums of lactate [ 1 & A ; 3 ] . Conventionally, lactate is produced from lactic acid bacteriums in which LDH converts pyruvate to breastfeed [ 3 ] .

But this method is less economic due to expensive purification processs required and the lactate produced as a consequence is less acid-tolerant [ 3 ] . An alternate and improved method uses barms to bring forth the lactate by agitation procedure [ 1 & A ; 3 ] . Colombi et Al. and Branduardi et Al showed how LDH can be used to bring forth lactate from barm [ 1 & A ; 3 ] . They integrated LDH cistron from Lactobacillus Plantarum into genome of metabolically engineered barm Saccharomyces cerevisiae. “ The LDH cistron look in a budding barm cell introduces a novel and alternate tract for the NAD + regeneration, leting a direct decrease of the intracellular pyruvate to breastfeed, taking to a coincident accretion of lactate and ethyl alcohol ” [ 1 ] .

Due to its efficiency, utmost stableness to thermal denaturation and low cost, LDH has besides found its utilizations in pharmaceautical industry to bring forth chirally pure? -lactate which is used to bring forth a big assortment of pharmaceuticals such as antihypertensives, semi-synthetic pencillins etc. It besides has medicative utilizations and is used as a diagnostic assistance in PKU [ 10 ] . However, LDH requires stoichiometric sums of NADH which is a really expensive cofactor. Therefore, NADH has to be recycled to do the procedure cost-efficient. For this intent, the dehydrogenase of pick is “ formate dehydrogenase ” ( FDH ) , since it is more stable and has a comparatively high activity.

Besides, the reduction agent “ formate ” is inexpensive and the oxidised merchandise “ CO2 ” can be removed easy from the reaction and therefore NADH is reduced wholly [ 10 & A ; 19 ] . Furthermore, LDH besides requires an allosteric activator “ fructose 1,6-bisphospate ” ( FBP ) for its maximum activity and has limited substrate specificity [ 10 ] . Karaguler et Al. employed protein technology to better the belongingss of LDH and to get the better of the disadvantages it shows in large-scale production of chirally pure lactate [ 10 ] . They used a Deoxyribonucleic acid scuffling attack to bring forth a mutation shuffled bsLDH, whose substrate specificity is now switched from pyruvate/lactate to malate/oxaloacetate and it no longer requires FBP for its activity [ 10 ] .

Another application of LDH is its usage as a accelerator in organic synthesis. Simon et Al. found L-LDH really utile in organic synthesis due to the fact that it can change over a broad scope of 2-oxoacids into S-2-hydroxy acids [ 19 ] . They besides attempted to do a comparing between utility of L-LDH and D-LDH for usage in organic synthesis [ 19 ] . They observed that L-LDH was relatively more utile in this respect as compared to D-LDH since the later shows narrower substrate specificity [ 19 ] .

Lactate dehydrogenase check is used for cell proliferation trial in a civilization in order to step and analyze the increased figure of cells as a consequence of cell division and cell growing [ 17 ] .

LDH in Nanotoxicology:

LDH check is besides widely used in nanotoxicology for the showing of in vitro cytotoxicity ensuing in cell harm. Nanotoxicity leads to cell membrane harm. Once the cell membrane is damaged, the cytoplasmatic enzymes, including LDH, are released. From the sum of LDH released, the extent of cell toxicity can be measured. A fluogenic index such as resazurin can be used to mensurate this LDH release from the damaged cells. “ Released LDH transportations lactate to pyruvate with co-reaction of NAD+ to NADH passage, and so the oxidization reaction of NADH to NAD+ transportations the non fluorescent resazurin to ruddy fluorescent resorufin. Feasible cells, nevertheless, produce negligible fluorescent signal with LDH check ” [ 25 ] . Thus the fluorescent signal of merely the damaged cells can be measured which can be used in observing the extent of cytotoxicity [ 25 ] .


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  2. Butova, O.A. & A ; Masalov, S.V. ( 2009 ) , “ Lactate dehydrogenase activity as an index of musculus tissue metamorphosis in extremely trained jocks ” , Human Physiology, vol. 35, no. 1, pp. 127-129.
  3. Colombi, S. & A ; Sablayrolles, J. ( 2004 ) , “ Nicotinic acid controls lactate production by K1-LDH: a Saccharomyces cerevisiae strain showing a bacterial LDH cistron ” , J Ind Microbiol Biotechnol, vol. 31, pp. 209-215.
  4. Ebyen, F.E. ( 2001 ) , “ A systematic reappraisal of lactate dehydrogenase isoenzyme 1 and germ cell tumours ” , Clinical Biochemistry, vol. 34, pp. 441-454.
  5. Ellis, G. P. & A ; West, G. B. ( 1976 ) , Progress in medicative chemical science 13, Elsevier.
  6. Elmhurst College, Role of enzymes in biochemical reactions. Available from: Elmhurst College, Illinois, Web site: hypertext transfer protocol: // [ Accessed: November 10, 2009 ] .
  7. Feder, M. E. , Bennett, A. F. & A ; Burggren, W. W. & A ; Huey, R. B. ( 1988 ) , New waies in ecological physiology, Cambridge University Press.
  8. Graham L. Patrick. ( 2009 ) . Enzymes: Structure and Function. An Introduction to Medicinal Chemistry. 4th edition. New York: Oxford University Press Inc. p30-41.
  9. Hummel, W. , Schfitte, H. & A ; Kula, M. ( 1983 ) , “ Large scale production of D-lactate dehydrogenase for the stereospecific decrease of pyruvate and phenyipyruvate ” , European Journal of Applied Microbiology and Biotechnology, vol. 18, no. pp. 75-85.
  10. Karaguler, N.G. , Sessions, R.B. & A ; Binay, B. ( 2007 ) , “ Protein technology applications of industrially exploitable enzymes: Geobacillus stearothermophilus LDH and Candida methylica FDH ” , Biochemical Society Transactions, vol. 35, pp. 1610-1615.
  11. Katakis, I. & A ; Domlnguez, E. ( 1997 ) , “ Fundamental reappraisal catalytic electrooxidation of NADH for dehydrogenase amperometric biosensors ” , Mikrochimica Acta, vol. 126, no. pp. 11-32.
  12. Koolman, J. & A ; Roehm, K. M. ( 2005 ) , Color Atlas of biochemistry, 2nd erectile dysfunction, Georg Thieme Verlag.
  13. Latner, A.L. ( 1970 ) , “ The nature of isoenzymes ” , Journal of Clinical Pathology, vol. 4, pp. 8-13.
  14. Linfield College, Lactate dehydrogenase: enzyme extraction, purification, and kinetic behaviour. Available from: Linfield College, Web site: hypertext transfer protocol: // % 20440/Lactate_Dehydrogenase.pdf [ Accessed: November 11, 2009 ] .
  15. Liu, Z. , Lee, S. , Sarun, S. , Peschel, D. & A ; Groth, T. ( 2009 ) , “ Immobilization of poly ( ethylene imine ) on poly ( L-lactide ) promotes MG63 cell proliferation and map ” , Journal of Materials Science: Materials in Medicine, vol. 20, no. 11, pp. 2317-2326.
  16. Pantazis, P. , Lazarou, S.A. & A ; Papadopoulos, N.M. ( 1981 ) , “ Isoenzymes of lactate dehydrogenase in human leukemic cells in civilization treated inducers of distinction ” , The Journal of Cell Biology, vol. 90, pp. 396-401.
  17. Roche Applied Science, Apoptosis, cell Death and cell proliferation. Available from: hypertext transfer protocol: // [ Accessed: December 11, 2009 ] .
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  19. Simon, E.S. , Plante, R. & A ; Whitesides, G.M. ( 1989 ) , “ D-Lactate dehydrogenase: substrate specificity and usage as a accelerator in the synthesis of homochiral 2-hydroxy acids ” , Applled Biochemistry and Biotechnology, vol. 2, no. pp. 169-179.
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