Effect of melatonin on enzyme activities of glutathione reductase from human erythrocytes in vitro and from rat erythrocytes in vivo

2006 ◽  
Vol 537 (1-3) ◽  
pp. 59-63 ◽  
Author(s):  
Mustafa Erat ◽  
Mehmet Ciftci
Keyword(s):  
Glutathione Reductase ◽  
Enzyme Activities ◽  
Human Erythrocytes ◽  
Rat Erythrocytes

scholarly journals Effects of Gentamicin Sulfate on Enzyme Activities of Carbonic Anhydrase from Human Erythrocytes in Vitro and from Rat Erythrocytes in Vivo

2002 ◽  
Vol 25 (8) ◽  
pp. 966-969 ◽  
Author(s):  
Sükrü Beydemir ◽  
Mehmet Çiftçi ◽  
Ömer Irfan Küfrevioglu ◽  
Mehmet Emin Büyükokuroglu
Keyword(s):  
Carbonic Anhydrase ◽  
Enzyme Activities ◽  
Human Erythrocytes ◽  
Rat Erythrocytes ◽  
Gentamicin Sulfate

Effects of some medical drugs on enzyme activities of carbonic anhydrase from human erythrocytes in vitro and from rat erythrocytes in vivo

2000 ◽  
Vol 42 (2) ◽  
pp. 187-191 ◽  
Author(s):  
Şükrü Beydemir ◽  
Mehmet Çİftçi ◽  
İsmail Özmen ◽  
Mehmet Emin Buyuk Okuroglu ◽  
Hasan Özdemir ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Enzyme Activities ◽  
Human Erythrocytes ◽  
Rat Erythrocytes

scholarly journals Surface-Engineered Dendrimeric Nanoconjugates for Macrophage-Targeted Delivery of Amphotericin B: Formulation Development andIn VitroandIn VivoEvaluation

2015 ◽  
Vol 59 (5) ◽  
pp. 2479-2487 ◽  
Author(s):  
Keerti Jain ◽  
Ashwni Kumar Verma ◽  
Prabhat Ranjan Mishra ◽  
Narendra Kumar Jain
Keyword(s):  
Drug Release ◽  
Amphotericin B ◽  
Human Erythrocytes ◽  
Antileishmanial Activity ◽  
Cell Uptake ◽  
Antiparasitic Activity ◽  
Content Type ◽  
Drug Localization

ABSTRACTThe present study aimed to develop an optimized dendrimeric delivery system for amphotericin B (AmB). Fifth-generation (5.0G) poly(propylene imine) (PPI) dendrimers were synthesized, conjugated with mannose, and characterized by use of various analytical techniques, including Fourier transform infrared spectroscopy (FTIR),1H nuclear magnetic resonance (1H-NMR) spectroscopic analysis, and atomic force microscopy (AFM). Mannose-conjugated 5.0G PPI (MPPI) dendrimers were loaded with AmB and evaluated for drug loading efficiency,in vitrodrug release profile, stability, hemolytic toxicity to human erythrocytes, cytotoxicity to and cell uptake by J774A.1 macrophage cells, antiparasitic activity against intracellularLeishmania donovaniamastigotes,in vivopharmacokinetic and biodistribution profiles, drug localization index, toxicity, and antileishmanial activity. AFM showed the nanometric size of the MPPI dendrimers, with a nearly globular architecture. The conjugate showed a good entrapment efficiency for AmB, along with pH-sensitive drug release. Highly significant reductions in toxicity toward human erythrocytes and macrophage cells, without compromising the antiparasitic activity of AmB, were observed. The dendrimeric formulation of AmB showed a significant enhancement of the parasiticidal activity of AmB toward intramacrophagicL. donovaniamastigotes. In thein vitrocell uptake studies, the formulation showed selectivity toward macrophages, with significant intracellular uptake. Further pharmacokinetic and organ distribution studies elucidated the controlled delivery behavior of the formulation. The drug localization index was found to increase significantly in macrophage-rich organs.In vivostudies showed a biocompatible behavior of MPPIA, with negligible toxicity even at higher doses, and promising antileishmanial activity. From the results, we concluded that surface-engineered dendrimers may serve as optimized delivery vehicles for AmB with enhanced activity and low or negligible toxicity.

scholarly journals Antigenicity of the infected-erythrocyte and merozoite surfaces in Falciparum malaria.

1979 ◽  
Vol 150 (5) ◽  
pp. 1241-1254 ◽  
Author(s):  
S G Langreth ◽  
R T Reese
Keyword(s):  
Plasmodium Falciparum ◽  
Falciparum Malaria ◽  
Infected Erythrocyte ◽  
Falciparum Infection ◽  
Human Erythrocytes ◽  
Cross Linking ◽  
Common Antigens

The antigenicity of altered structures induced by Plasmodium falciparum in the membranes of infected Aotus monkey and human erythrocytes was examined. Antisera were obtained from monkeys made immune to malaria. Bound antibodies were shown to be localized on the knob protrusions of infected erythrocytes of both human and monkey origin and from both in vitro and in vivo infections. Therefore, P. falciparum infection has produced similar antigenic changes in the erythrocyte surfaces of both man and monkey. Uninfected erythrocytes and all knobless-infected erythrocytes bound no antibody from immune sera. Strains of P. falciparum from widely different geographic areas that were cultured in vitro in human erythrocytes induced structures (knobs) which have common antigenicity. Merozoites were agglutinated by cross-linking of their cell coats when incubated with immune sera. The binding of ferritin-labeled antibody was heavy on the coats of both homologous and heterologous strains of the parasite, indicating that the merozoite surfaces of these strains share common antigens.

Oxidative activity of primaquine metabolites on rat erythrocytes IN vitro and in vivo

1994 ◽  
Vol 47 (2) ◽  
pp. 309-316 ◽  
Author(s):  
Jeannette Vásquez-Vivar ◽  
Ohara Augusto
Keyword(s):  
Oxidative Activity ◽  
Rat Erythrocytes
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