Malarial parasite metabolism: The lactic acid dehydrogenase of Plasmodium berghei

Langer, Bernhardt W.; Phisphumvidhi, Pirom; Jiampermpoon, Duangduen

doi:10.1016/0014-4894(69)90218-5

Cited by 12 publications

(5 citation statements)

References 6 publications

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“…It is interesting to note that the apparent Km (pyruvate) for LDH of i? berghei (58 ^M, Phisphumvidhi andLanger, 1969) andP. falciparum (30 iiM, Vander et al, 1981) is in the range observed in the present investigation for P. knowlesi LDH, and is quite different from LDH of mouse erythrocytes (160 ^M, Phisphumidhi and Langer, 1969) and monkey erythrocytes (140 ^M).…”

Section: Properties Of Purified Lactate Dehydrogenasesupporting

confidence: 51%

“…The NADH requirement for LDH of P. knowlesi and monkey erythrocytes is almost equal although Phisphumvidhi and Langer (1969) reported a difference in Km (NADH) for LDH from P. berghei and mouse erythrocytes, further indicating the species differences of various hosts and parasites. LDH from P. knowlesi and monkey erythrocytes exhibit optimal activity at pH 6-8 and 7-5, respectively, whereas the enzyme from P. lophurae and duck erythrocytes showed maximum activity at approximately pH 7-4 (Sherman, 1961).…”

Section: Discussionmentioning

confidence: 96%

Section: Properties Of Purified Lactate Dehydrogenasementioning

confidence: 96%

“…Several reports are available regarding the differences in the electrophoretic behaviour of plasmodial LDH and the analogous enzyme of their respective hosts (Sherman, 1961;Phisphumvidhi and Langer, 1969;Momen, 1979;Saxena et al, 1982). The present study confirms the fact that the electrophoretic mobility of P. knowlesi LDH is different from the host enzyme.…”

Section: Properties Of Purified Lactate Dehydrogenasementioning

confidence: 99%

“…The presence of lactate dehydrogenase (1-lactate: NAD + oxidoreductase, E.C.I.1.1.27), the terminal enzyme of anaerobic glycolysis, has been reported in several plasmodial species, viz., Plasmodium berghei (Phisphumvidhi and Langer, 1969) and P. lophurae (Sherman, 1961;1962). However, no attempts have been made to purify plasmodial LDH and compare its properties with the corresponding enzyme from host red cells.…”

Section: Introductionmentioning

confidence: 99%

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PURIFICATION AND PROPERTIES OF LACTATE DEHYDROGENASE FROM PLASMODIUM KNOWLESI AND ERYTHROCYTES OF THE RHESUS MONKEY

Saxena

Pandey

et al. 1986

Aust J Exp Biol Med

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Summary Lactate dehydrogenase, E.C.1.1.1.27 (LDH) from the simian malarial parasite, Plasmodium knowlesi, and from normal rhesus monkey erythrocytes has been purified using Blue Sepharose affinity chromatography, and the properties of the purified enzyme from these two sources have been compared. The enzyme from the host and parasite were different in their kinetic properties, viz., substrate and pH optima, thermostability and isoenzymic behaviour. Partially purified LDH of the erythrocytes resolved into three isomeric bands on polyacrylamide gel electrophoresis, whereas the parasite LDH moved as a single enzyme band of different mobility from the host LDH. The molecular mass of the parasite enzyme was estimated as 117,500 daltons.

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Section: Properties Of Purified Lactate Dehydrogenasesupporting

confidence: 51%

Section: Discussionmentioning

confidence: 96%

Section: Properties Of Purified Lactate Dehydrogenasementioning

confidence: 96%

Section: Properties Of Purified Lactate Dehydrogenasementioning

confidence: 99%