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Original Article

Purification and characterization of a 33 kDa serine protease from Acanthamoeba lugdunensis KA/E2 isolated from a Korean keratitis patient

Hyo-Kyung Kim1, Young-Ran Ha2, Hak-Sun Yu2, Hyun-Hee Kong2, Dong-Il Chung2
The Korean Journal of Parasitology 2003;41(4):189-196.
Published online: December 20, 2003

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Corresponding author (dichung@knu.ac.kr)
• Received: September 23, 2003   • Accepted: November 17, 2003

Copyright © 2003 by The Korean Society for Parasitology

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Purification and characterization of a 33 kDa serine protease from Acanthamoeba lugdunensis KA/E2 isolated from a Korean keratitis patient
Korean J Parasitol. 2003;41(4):189-196.   Published online December 20, 2003
DOI: https://doi.org/10.3347/kjp.2003.41.4.189
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Purification and characterization of a 33 kDa serine protease from Acanthamoeba lugdunensis KA/E2 isolated from a Korean keratitis patient
Korean J Parasitol. 2003;41(4):189-196.   Published online December 20, 2003
DOI: https://doi.org/10.3347/kjp.2003.41.4.189
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Purification and characterization of a 33 kDa serine protease from Acanthamoeba lugdunensis KA/E2 isolated from a Korean keratitis patient
Image Image Image Image Image
Fig. 1 Chromatograms of proteinase purification from the culture supernatant of Acanthamoeba lugdunensis KA/E2. A. CM-Sepharose chromatography of the ammonium sulfate-precipitated culture supernatant. B. Chromatogram of Sephacryl S-200 column of the enzymatically active fractions (fractions 36-42) from A. C. Chromatogram of enzymatically active fractions (fraction numbers 28-31) of B from a mono Q anion-exchange column.
Fig. 2 SDS-PAGE of the purified enzyme in a gradient acrylamide gel. A single protein band (arrow) stained with Coomassie blue was observed with a size of approximately 33 kDa. Lane: M, standard size marker: P, purified proteinase.
Fig. 3 Effect of pH and temperature on serine proteinase activity. A. The enzyme activity was assayed in sodium acetate (pH 5.5-6.0), phosphate (pH 6.0-8.0), or Tris-HCl (pH 8.0-10.0). B. Optimum temperature of the enzyme. Enzyme activity is expressed as a percentage of the maximum proteolytic activity observed.
Fig. 4 Substrate specificity of the purified secretory serine proteinase of A. lugdunensis KA/E2. M, protein size standard; Lane 1, reaction mixture without enzyme; 2-4, incubation for 30 sec, 10 min, 30 min; M, protein size standard. Marks indicate α-chains of type I collagen (▶) monomers (➡) and dimers (⇨) of hemoglobin.
Fig. 5 Degradation of IgG and IgA by the serine proteinase of A. lugdunensis KA/E2. Lane 1, reaction mixture without enzyme; 2-4, incubation for 30 sec, 10 min, 30 min; M, protein size. The heavy (▶) and light chains (▷) of immunoglobulins are indicated.

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Fig. 5

Purification and characterization of a 33 kDa serine protease from Acanthamoeba lugdunensis KA/E2 isolated from a Korean keratitis patient
  Step Total protein (mg) Total activity (μg/min) Specific activity (μg/min/mg) Purification (fold) Yield (%)
Culture supernatant 156.3 813.0 5.2 1.0 100.0
Ammonium sulfate precipitation 28 770.0 27.5 5.3 94.7
CM-Sepharose 3.65 243.1 66.6 12.8 29.9
Sephacryl S-200 0.25 142.6 570.3 109.7 17.5
Q-anion exchange 0.03 26.1 814.4 156.6 3.2
 Inhibitor/activator Final Concentration Activity as percent of control
Control 100.0
Serine class
 PMSF 1 mM 6.9
 DFP 1 mM 15.9
Cysteine class
 E-64 10 μg/ml 96.7
 DTT 1 mM 85.5
Aspartic class
 Pepstatin A 1 μg/ml 97.4
Metallo class
 EDTA 1 mM 108.3
 1, 10-Phenanthroline 1 mM 107.2
Table 1. Purification steps of the serine proteinase obtained from the culture supernatant of Acanthamoeba lugdunensis KA/E2
Table 2. Effects of enzyme inhibitors and activators on the activity of the purified proteinase

Table 1.

Table 2.

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