Strain-rate dependent material properties of the porcine and human kidney capsule

This study was performed to characterize the mechanical properties of the kidney capsular membrane at strain-rates associated with blunt abdominal trauma. Uniaxial quasi-static and dynamic tensile experiments were performed on fresh, unfrozen porcine and human renal capsules at deformation rates ranging from 0.0001 to 7 m/s (strain-rates of 0.005-250 s(-1)). Single stroke, dynamic tests were performed on samples of porcine renal capsule at strain-rates of 0.005 s(-1) (n = 33), 0.05 s(-1) (n = 17), 0.5 s(-1) (n = 38), 2 s(-1) (n = 10), 4 s(-1) (n = 10), 50 s(-1) (n = 21), 100 s(-1) (n = 18), 150 s(-1) (n = 17), 200 s(-1) (n = 10), and 250 s(-1) (n = 17). Due to limited availability of human tissues, only quasi-static tests were performed (0.005 s(-1), n = 25). Porcine renal capsule properties were found to match the material properties of human capsular tissue sufficiently well such that porcine tissue material can be used as a human test surrogate. The apparent elastic modulus and breaking stress of the porcine renal capsule were observed to increase significantly with increasing strain-rate (p < 0.01). Breaking strain was inversely related to strain-rate (p < 0.01). The effect of increasing strain-rate on material properties diminished appreciably at rates exceeding 150 s(-1). Empirically derived mathematical models of constitutive behavior were developed using a hyperelastic/viscoelastic Ogden formulation, as well as a Cowper-Symonds law material curve multiplication.     

On the origins of esterases

Comparisons among the primary sequences of five cloned eukaryotic esterases reveal two distinct lineages, neither bearing any significant overall sequence similarity to the functionally related serine protease multigene family. We have not eliminated the possibility that the esterases may have residual conformational similarities to the serine proteases. However, our profile analysis and analyses of the predicted conformations of the esterases reveal little similarity to the serine proteases. Four of the esterase proteins share 27%-53% overall sequence similarity and evidence of a catalytic mechanism involving the same Arg- Asp-Ser or His-Asp-Ser charge relay. We propose that these four esterases, three of them cholinesterases, form part of a multigene family essentially separate from the serine proteases.