Galan Guzman

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 This study investigates a mutant barnacle troponin C (TnC) protein (BTnC2–4-) in which the Ca2+-binding sites (sites II and IV) have been rendered non-functional. Eliminating Ca2+ binding at both Ca2+-binding sites of barnacle TnC did not prevent the incorporation of BTnC2–4- into TnC-depleted myofibrillar bundles, although, as expected, the mutant was not(More)
To examine the importance of the central α-helix of troponin C (TnC) we have bacterially expressed one of the isoforms of barnacle TnC (BTnC2), BTnCWT, but without the aspartate residue at position 80 in the central helix (BTnC80–). This manipulation is expected to produce an approximately 100° axial rotation of the C-domain with respect to the N-domain,(More)
Mouse monoclonal antibodies (MAbs) were raised to dengue-2 virus (D-2V) Cuban (A15) strain and the cell culture supernatants were screened by ELISA using the homologous virus. Three MAb-secreting lines were further characterized using immunoblot, haemaglutination, complement-fixation, and neutralization assays. One of these, MAb 8H8, weakly reacted with the(More)
Semi-purified DEN-4 envelope protein, obtained in Pichia pastoris, was capable of generating neutralising and protecting antibodies after immunisation in mice. Here we compared two purification processes of this recombinant protein using two chromatographic steps: immune-affinity chromatography and immobilised metal ion adsorption chromatography (IMAC). The(More)
The phosphorylation of the internal and integral membrane (M1) protein of influenza virus was studied. Four points can be made based on the data: (1) The M1 contains at least two moles of phosphate per mole of M1. (2) Phosphorylation of M1 is conserved between influenza A, B and C viruses. Other characteristics of the M1 are also conserved, such as(More)
A mouse monoclonal antibody (MAb, 4B6) was able to recognize dengue virus type 4 envelope (E) protein both as a recombinant protein in Pichia pastoris and when it was present in infected brains of suckling mice. 4B6 was characterized by enzyme-linked immunoadsorbent assay (ELISA), hemaglutination inhibition, neutralization, and immunoblot. The MAb was(More)
Two genetically engineered, recombinant versions of native barnacle troponin C (TnC) (BTnC2) were created from the bacterially expressed, recombinant, wild-type BTnC (BTnCWT) to investigate the role of the Ca2+-specific sites in force regulation. The mutant BTnC4– contains a single amino acid mutation in site IV which results in the inactivation of site IV(More)
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