Lipid thermotropic transitions in Triatoma infestans lipophorin

The structure and lipid thermotropic transitions of highly purified lipophorin of Triatoma infestam were examined by several techniques: steady-state fluorescence polarization of 1,6-diphenyl-1,3,5-hexatrien(eD PH), cis-parinaric acid (cis-PnA) and tram-parinaric acid (tram-PnA), light scattering fl...

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Autores principales: Soulages, Jose Luis, Rimoldi, Omar Jorge, Brenner, Rodolfo Roberto
Formato: Articulo
Lenguaje:Inglés
Publicado: 1989
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Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/120436
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id I19-R120-10915-120436
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Médicas
Fluorescence probes
Diacylglycerol
Phospholipids
Fluorescence polarization
spellingShingle Ciencias Médicas
Fluorescence probes
Diacylglycerol
Phospholipids
Fluorescence polarization
Soulages, Jose Luis
Rimoldi, Omar Jorge
Brenner, Rodolfo Roberto
Lipid thermotropic transitions in Triatoma infestans lipophorin
topic_facet Ciencias Médicas
Fluorescence probes
Diacylglycerol
Phospholipids
Fluorescence polarization
description The structure and lipid thermotropic transitions of highly purified lipophorin of Triatoma infestam were examined by several techniques: steady-state fluorescence polarization of 1,6-diphenyl-1,3,5-hexatrien(eD PH), cis-parinaric acid (cis-PnA) and tram-parinaric acid (tram-PnA), light scattering fluorescence energy transfer between the lipophorin tryptophan residues and the bound chromophores, DPH, tram-parinaric acid cis-parinaric acid, gel electrophoresis, and gel filtration. Fluorescence polarization of PnAs and DPH revealed a reversible lipid thermotropic transition in intact lipophorin at about 2OoC and 18OC, respectively. In lipophorin, lipid dispersion fluorescence polarization of DPH detected a lipid transition approximately at 2OoC, while tram-PnA showed a gel phase formation at a temperature below 3OOC. Similar experiments in which tram-PnA was incorporated into diacylglycerols and phospholipids extracted from the lipophorin revealed gel phase formation below 3OoC and 24OC, respectively. Light scattering measurements showed that lipophorin particles aggregate irreversibly at 45OC, increasing the molecular weight, as determined by gel filtration on Sephacryl S-300, from 740,000 to values larger than 1,500,000. The particle aggregation did not change the physical properties of the lipophorin studied by fluorescence polarization, indicating that the aggregation is apparently a non-denaturing process. Energy transfer between the lipophorin tryptophans and the bound chromophores cis-PnA, tram-PnA, and DPA revealed a different locationo f the fluorescent probes within thleip ophorin. Temperature-dependence on the energy transfer efficiency for all probes confirmed a change in the ordering of the lipophorin lipids at 24'C-
format Articulo
Articulo
author Soulages, Jose Luis
Rimoldi, Omar Jorge
Brenner, Rodolfo Roberto
author_facet Soulages, Jose Luis
Rimoldi, Omar Jorge
Brenner, Rodolfo Roberto
author_sort Soulages, Jose Luis
title Lipid thermotropic transitions in Triatoma infestans lipophorin
title_short Lipid thermotropic transitions in Triatoma infestans lipophorin
title_full Lipid thermotropic transitions in Triatoma infestans lipophorin
title_fullStr Lipid thermotropic transitions in Triatoma infestans lipophorin
title_full_unstemmed Lipid thermotropic transitions in Triatoma infestans lipophorin
title_sort lipid thermotropic transitions in triatoma infestans lipophorin
publishDate 1989
url http://sedici.unlp.edu.ar/handle/10915/120436
work_keys_str_mv AT soulagesjoseluis lipidthermotropictransitionsintriatomainfestanslipophorin
AT rimoldiomarjorge lipidthermotropictransitionsintriatomainfestanslipophorin
AT brennerrodolforoberto lipidthermotropictransitionsintriatomainfestanslipophorin
bdutipo_str Repositorios
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