Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 394-399 |
| Number of pages | 6 |
| Journal | Experimental Parasitology |
| DOIs | |
| Publication status | Published - 1 Aug 2010 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Parasitology
- Immunology
- Infectious Diseases
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Entamoeba histolytica: Soluble and membrane-associated neutral sphingomyelinase-C and other unidentified esterase activity. / Vargas-Villarreal, Javier; Palacios-Corona, Rebeca; Hernández-Luna, Carlos; Mata-Cárdenas, Benito David; Torres de la Cruz, Victor M.; Cortés-Gutiérrez, Elva I.; González-Salazar, Francisco; Garza-González, Jesús Norberto; Escobedo-Guajardo, Brenda Leticia; Said-Fernández, Salvador.
In: Experimental Parasitology, 01.08.2010, p. 394-399.Research output: Contribution to journal › Article
TY - JOUR
T1 - Entamoeba histolytica: Soluble and membrane-associated neutral sphingomyelinase-C and other unidentified esterase activity
AU - Vargas-Villarreal, Javier
AU - Palacios-Corona, Rebeca
AU - Hernández-Luna, Carlos
AU - Mata-Cárdenas, Benito David
AU - Torres de la Cruz, Victor M.
AU - Cortés-Gutiérrez, Elva I.
AU - González-Salazar, Francisco
AU - Garza-González, Jesús Norberto
AU - Escobedo-Guajardo, Brenda Leticia
AU - Said-Fernández, Salvador
PY - 2010/8/1
Y1 - 2010/8/1
N2 - Sphingomyelinase (SMase) activity was measured in Entamoeba histolytica particulate and soluble subcellular fractions. The effects on SMase of incubation time, total protein concentration, pH, and several divalent cations were determined. SMase-C and other unidentified esterase activity were detected in soluble and particulate fractions. SMase-C was 94.5-96.0% higher than the unidentified esterase activity. Soluble and insoluble SMase-C specific activities increased with protein dose and incubation time. Soluble and insoluble SMase-C activities were maximum at pH 7.5 and were dependent on Mg2+, Mn2+, or Co2+, and inhibited by Zn2+, Hg2+, Ca2+, and EDTA. SMase-C was active in the pH range of 3-10 and its maximum activity was at pH 7.5. The soluble and insoluble SMases have remarkably similar physicochemical properties, strongly suggesting that E. histolytica has just one isoform of neutral SMase-C that had not been described before and might be essential for E. histolytica metabolism or virulence. © 2010 Elsevier Inc.
AB - Sphingomyelinase (SMase) activity was measured in Entamoeba histolytica particulate and soluble subcellular fractions. The effects on SMase of incubation time, total protein concentration, pH, and several divalent cations were determined. SMase-C and other unidentified esterase activity were detected in soluble and particulate fractions. SMase-C was 94.5-96.0% higher than the unidentified esterase activity. Soluble and insoluble SMase-C specific activities increased with protein dose and incubation time. Soluble and insoluble SMase-C activities were maximum at pH 7.5 and were dependent on Mg2+, Mn2+, or Co2+, and inhibited by Zn2+, Hg2+, Ca2+, and EDTA. SMase-C was active in the pH range of 3-10 and its maximum activity was at pH 7.5. The soluble and insoluble SMases have remarkably similar physicochemical properties, strongly suggesting that E. histolytica has just one isoform of neutral SMase-C that had not been described before and might be essential for E. histolytica metabolism or virulence. © 2010 Elsevier Inc.
U2 - 10.1016/j.exppara.2010.03.010
DO - 10.1016/j.exppara.2010.03.010
M3 - Article
SP - 394
EP - 399
JO - Experimental Parasitology
JF - Experimental Parasitology
SN - 0014-4894
ER -