L. D. Allhouse

Learn More
 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)
 Incubation of mechanically skinned barnacle myofibrillar bundles in 10 mM orthovanadate (pH 6.6) results in the loss of Ca2+-dependent force generation, which reduces to 0.98±0.006% (mean ±SEM, n=25) of control levels. Analysis of myofibrillar bundles by gel electrophoresis showed that tension loss is primarily due to the extraction of troponin C (TnC)(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)
 The aim of this study was to compare the effects of increased concentrations of MgADP, inorganic phosphate (Pi) and H+ ([MgADP], [Pi] and [H+], respectively) on the rate of relaxation in two different muscle types: skinned muscle fibres from the frog Rana temporaria and myofibrillar bundles from the giant Pacific acorn barnacle Balanus nubilus. Relaxation(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)
  • 1