Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 3 de 3
Filter
Add filters








Year range
1.
Journal of Gorgan University of Medical Sciences. 2008; 10 (1): 61-66
in Persian | IMEMR | ID: emr-87857

ABSTRACT

Despite their very wide geographical distribution in the Mediterranean region, most Leishmania infantum strains belong to zymodeme MON-1. As different Leishmania species are known to cause different clinical symptoms and may require different treatment protocols, therefore this study was done to identify and characterize the leishmania agents causing visceral, Leishmaniasis [VL] in humans, reservoirs and vectors in the north-west of Iran by Isoenzyme analyses. In this descriptive and cross sectional study, The samples collected from 12 VL confirmed patients [bone marrow aspirates], 26 dogs [spleen and hepatic aspirates] and more than 100 sand flies from northwest of Iran between 2005 and 2006. All aspirated material from human, canine and sandflies demostrated growth of Leishmania parasite in NNN and ?MEM media. The above species compared with WHO reference strains, Leishmania [Leishmania] donovani [DD8], L [L] infantum [IPT-1], L [L] tropica [K-27], and L[L] major [5-ASKH], using thin layer starch gel electrophoresis. The enzymes investigated in this study were ALAT, ASAT, SOD, ES,NH, MPI, GPI, MDH, 6PGD, PGM, PEPD, and PDK In this study L.infuntum. MON-1 was the only zymodeme present in all samples of dogs and human sandflies. We concluded that the visceral Leishmania [VL] focus in northwest of Iran is evidently Mediterranean type, which extends from Portugal and Morocco to Pakistan and the Central Asia and domestic doges act as the reservoir host in northwest of Iran, where the complete life cycle of zymodeme MON-1 has been identified


Subject(s)
Humans , Animals , Disease Reservoirs , Disease Vectors , Electrophoresis , Cross-Sectional Studies
2.
Medical Journal of the Islamic Republic of Iran. 2005; 19 (2): 169-174
in English | IMEMR | ID: emr-171183

ABSTRACT

Dietary antioxidant intake has been reported to be inversely associated with coronary artery disease. To clarify the possible role of lipophilic antioxidants in the prevention of atherosclerosis, we investigated the effects of ubiquinol-10 and beta-carotene on the susceptibility of low-density lipoprotem [LDL] to oxidative modification. In this study, first "ubiquinol-10 and beta-carotene" were added to plasma and incubated for 3hr at 37°C. Then, the LDL fraction was separated by ultracentrifugation. The oxidizability of LDL was estimated by measuring conjugated diene[CD], lipid peroxides and thiobarbituric acid-reactive substances [TEARS] after cupric sulfate solution was added. We showed that ubiquinone-10 and P-carotene significantly [p<0.01 by ANOVA] and dose-dependently prolonged the lag time before initiation of oxidation reaction. Also, these two compounds suppressed the formation of lipid peroxides and TEARS more markedly than others. The ability of them to prolong lag time and suppression of lipid peroxides and TEARS formation resulted to be in the following order: ubiquinol-10> p-carotene.LDL exposed to the lipophilic antioxidants in vitro reduced oxidizability. These findings suggest that ubiquinol-10 and p-carotene have a role in ameliorating atherosclerosis

3.
IBJ-Iranian Biomedical Journal. 2002; 6 (1): 31-6
in English | IMEMR | ID: emr-59433

ABSTRACT

Cloning and expression of the L-phenylalanine dehydrogenase gene, from B. sphaericus in E. coli were done. The gene was cloned in the vector pET16b and transformed into E. coli BL21 [DE3]. The functional form of the L-phenylalanine dehydrogenase enzyme was purified by affinity purification techniques, taking advantage of the ability of this enzyme to bind to the nucleotide site affinity dye, Reactive Blue 4. Approximately 3 mg of highly purified recombinant enzyme was obtained from 950 mg cell pellet [wet weight]. The Relative molecular mass of the L-phenylalanine subunits was about 41 kDa by 10% SDS-PAGE. Using this method, the enzyme was obtained with a yield of 28%, and had a specific activity of 577.3 U/mg proteins, which is purified 88 times. This method was provided a facile and effective way for preparing the enzyme with a good yield that suitable for analytical purposes


Subject(s)
Gene Expression , Escherichia coli , Genetic Vectors , Phenylalanine Hydroxylase/genetics
SELECTION OF CITATIONS
SEARCH DETAIL