Warning: mkdir(): Permission denied in /home/virtual/lib/view_data.php on line 81
Warning: fopen(upload/ip_log/ip_log_2024-11.txt): failed to open stream: No such file or directory in /home/virtual/lib/view_data.php on line 83
Warning: fwrite() expects parameter 1 to be resource, boolean given in /home/virtual/lib/view_data.php on line 84 Studies on malic dehydrogenase activity in parasitic helminths
Studies on malic dehydrogenase activity in parasitic helminths
Eun Hee Lee and Byong Seol Seo
Department of Parasitology and Institute of Endemic diseases, College of Medicine, Seoul National University, Korea.
Abstract
The malic dehydrogenase activity was determined by the modified method of Ochoa (1955) using tissue homogenates of various parasitic helminths.
Worm parasites were mostly collected from local abattoir, and removed from the organ or tissues of the naturally infected animal hosts, and some materials were also obtained from the human hosts. The helminths used in this experiment include 3 kinds of nematodes, 5 kinds of trematodes, and 8 kinds of cestodes.
They were throughly washed and homogenized in glass tissue grinder in ice chilled water bath, and then centrifuged. The supernatants were designated as enzyme preparations. The hydrogen concentrations of buffer solution were pH 1.4, 2.7, 3.5, 4.2, 5.2, 7.4, 8.2, 9.3, 10.2, 11.6, and enzymatic reaction of this experiment was performed at incubation temperature of 20, 30, 40, and 50℃. The extinction of Nicotinamide Adenosine Dinucleotide (NAD) was measured by spectrophotometry at the wave length of 340 millimicron.
The results of the experiment were as follows:
1. The malic dehydrogenase activity occurred over all kinds of parasitic helminths used in this study. And the activity on sparganum turned out to be highest.
2. All helminths displayed their maximum activity in the range of alkaline pH.
3. A comparison of the effects of temperature and substrate concentration on the enzyme activity was made among these helminths. However, no definite relationship among them has been detected.
4. The significance of the existence of this enzyme in the helminths was briefly discussed.
Fig. 6 Relation between MDH activity and incubation temperature in nematodes.
Fig. 7 Relation between MDH activity and incubation temperature in trematodes.
Fig. 8 Relation between MDH activity and incubation temperature in cestodes (Cyclophyllidea).
Fig. 9 Relation between MDH activity and incubation temperature in larval and adult cestodes (Pseudophyllidea).
Fig. 10 Effects of the substrate concentration on the MDH activity in nematodes.
Fig. 11 Effects of the substrate concentration on the MDH activity in trematodes.
Fig. 12 Effects of the substrate concentration on the MDH activity in cestodes.
Tables
Table 1 Malic Dehydrogenase Activities in Various Parasitic Helminths (Changes in Optical Density per milligram nitrogen of worm tissue)
Table 2 Malic dehydrogenase activities in parasitic hilminths by the variation of incubation temperature. (Changes in O.D./mgN/min. of worm tissues)
Table 3 Malic dehydrogenase activities in parasitic hilminths by the variation of substrate concentration. (Changes in O.D./mgN/min. of worm tissue)
References
1.
Baernstein HD. Fed Proc 1952;11:183.
2.
Baernstein HD. Exp Parasit 1953;2:390–396.
3.
Baernstein HD. Malic dehydrogenase in Trichomonas vaginalis. J Parasitol 1961;47:279–284.
4.
Bryant C, et al. Exp Parasit 1960;12:342–376.
5.
Bueding E. Studies on the metabolism of the filarial worm, Litomosoides carinii. J Exp Med 1949;89(1):107–130.
6.
Bueding E, Charms B. Cytochrome c, cytochrome oxidase, and succinoxidase activities of helminths. J Biol Chem 1952;196(2):615–627.
7.
Conde-del Pino E, et al. Exp Parasit 1966;18:320–326.
8.
Dunagan TT, et al. J Parasit 1966;52:727–729.
9.
Goldberg E, et al. Am Zoologist 1963;3:486–489.
10.
Green DE. The malic dehydrogenase of animal tissues. Biochem J 1936;30(11):2095–2110.
11.
Grimm FC, Doherty DG. Properties of the two forms of malic dehydrogenase from beef heart. J Biol Chem 1961;236:1980–1985.
12.
Kaplan NO, Ciotti MM. Evolution and differentiation of dehvdrogenases. Ann N Y Acad Sci 1961;94:701–722.
13.
Kikuchi G, Ramirez J, Guzman Barron ES. Electron transport system in Ascaris lumbricoides. Biochim Biophys Acta 1959;36:335–342.
14.
Laufer H. Forms of enzymes in insect development. Ann N Y Acad Sci 1961;94:825–835.
15.
Lee SH. [Studies On Lactic Dehydrogenase Activity In Parasitic Helminths]. Korean J Parasitol 1967;5(1):5–16.
16.
Lowenthal A, Van Sande M, Karcher D. Heterogeneity of lactic and malic dehydrogenase in serum, cerebrospinal fluid, and brain extracts in man and sheep. Ann N Y Acad Sci 1961;94:988–995.
17.
Oda T. Jpn J Parasit 1963;12(4):267–281.
18.
Park CJ, Seo BS. [Studies On Phosphatase Activity In Some Parasitic Helminths]. Korean J Parasitol 1967;5(3):115–124.
19.
Rhodes MB, Marsh CL, Kelley GW Jr. Studies in Helminth Enzymology. 3. Malic Dehydrogenases of Ascaris Suum. Exp Parasitol 1964;15:403–409.
20.
Rhodes MB, Nayak DP, Kelley GW Jr, Marsh CL. Studies in Helminth Enzymology. IV. Immune Responses to Malic Dehydrogenase from Ascaris Suum. Exp Parasitol 1965;16:373–381.
21.
Saz HJ, Hubbard JA. The oxidative decarboxylation of malate by Ascaris lumbricoides. J Biol Chem 1957;225(2):921–933.
22.
Seidman I, Entner N. Oxidative enzymes and their role in phosphorylation in sarcosomes of adult Ascaris lumbricoides. J Biol Chem 1961;236:915–919.
23.
Siegel A, Bing RJ. Plasma enzyme activity in myocardial infarction in dog and man. Proc Soc Exp Biol Med 1956;91(4):604–607.
Ulmer DD, Vallee BL, Wacker WE. Metalloenzymes and myocardial infarction. II. Malic and lactic dehydrogenase activities and zinc concentrations in serum. N Engl J Med 1956;255(10):450–456.
28.
Williamson J. Observations on the dehydrogenase activity of normal and drug-resistant strains of Trypanosoma rhodesiense. Exp Parasitol 1953;2(4):348–357.
PDF Links
Full text via DOI
Download Citation 
