ABSTRACT
Estudou-se o perfil das proteínas da membrana externa (PME) da Leptospira interrogans sorovariedade Hardjoprajitno por meio da eletroforese bidimensional. Foram utilizadas técnicas de extração das PME com Triton x114 e precipitação com acetona. Os géis foram corados com nitrato de prata e as imagens analisadas para determinação da massa molecular das proteínas detectadas. Foram visualizadas 35 bandas protéicas, sendo que cinco delas se destacaram por estarem em maior quantidade: 22,54KDa (LipL22), 30/26KDa (LipL32), 34,41KDa (PME34), 42,75KDa (LipL41) e 58,59KDa (LipL63).
The protein profile of the outer membrane of Leptospira interrogans serovar Hardjoprajitno was determined by two-dimensional gel electrophoresis. The outer membrane was extracted with Triton x 114 and the proteins were precipitated with acetone. The images were analyzed for the determination of the molecular weight of the detected proteins. Thirty-five spots for the proteins that are predominant in the outer membrane of this Leptospira were observed and five proteins were found in higher quantities: 22.54KDa (LipL22), 30/26KDa (LipL32), 34.41KDa (PME34) (2), 42.75KDa (LipL41), and 58.59KDa (LipL63).
Subject(s)
Electrophoresis, Gel, Two-Dimensional/methods , Leptospira interrogans/ultrastructure , Membrane Proteins/classification , Membrane Proteins/chemistryABSTRACT
In polarized cells intracellular sorting of plasma membrane proteins occurs to a large extent at the trans-Golgi network, giving rise to vesicles destined for distinct plasma membrane domains. This review discusses the several pathways, both direct and indirect, which lead to protein incorporation into the correct cell surface, as well as the mechanisms involved. Proteins contain signals which direct their incorporation into the distinct vesicles destined for plasma membrane microdomains. Specific coat proteins are involved in vesicle assembly and are likely to play a role in the generation of discrete vesicle populations. Molecules involved in vesicle docking and fusion may also add specificity to the targeting process.
Subject(s)
Animals , Dogs , Cell Polarity , Membrane Proteins/metabolism , Coated Vesicles/physiology , Amino Acid Sequence , Biological Transport , Cell Line , Golgi Apparatus , Kidney , Membrane Fusion , Models, Biological , Molecular Sequence Data , Organelles , Protein Sorting Signals , Membrane Proteins/classification , Membrane Proteins/physiology , TyrosineSubject(s)
Animals , Membrane Proteins/classification , Coated Vesicles/metabolism , Biological Transport , Clathrin , Coatomer Protein , Guanosine Triphosphate , Macromolecular Substances , Models, Biological , Membrane Proteins/metabolism , Fungal Proteins/metabolism , Viral Proteins/metabolism , Saccharomyces cerevisiaeABSTRACT
Por la gran relevancia que tiene el glicocalix en la relación huésped-parásito, y para adentrarse en el conocimiento de las características y función que desempeña en diferentes parasitos, en este trabajo se aisló y caracterizó químicamente el glicocalix de cinco helmintos que tienen en común que, sin dividirse en el huésped, sobreviven en él durante mucho tiempo. En el glicocalix de ninguno de los parásitos estudiados se pudo demostrar la presencia de ácido siálico; en cambio, en todos se encontraron ácidos urónicos. En el glicocalix de los cinco parásitos estudiados, el cociente de azúcares sin carga/con carga y el de azúcares con carga negativa/positiva fue mayor de 1. En el glicocalix de Cysticercus celulasae y en el de Fasciola hepatica, los cocientes de azúcares con carga -negativa/positva y de azúcares/proteínas, fueron mayores que los de Ascaris suum, Macracanthorhynchus hirudinaceus y Moniezia expansa