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V Basso

Publications and source records attributed to V Basso.

3 recordsLinked to original sources

Functional integration approach to hysteresis.

A general formulation of scalar hysteresis is proposed. This formulation is based on two steps. First, a generating function g(x) is associated with an individual system, and a hysteresis evolution operator is defined by an appropriate envelope construction applied to g(x), inspired by the overdamped dynamics of systems evolving in multistable free-energy landscapes. Second, the average hysteresis response of an ensemble of such systems is expressed as a functional integral over the space G of all admissible generating functions, under the assumption that an appropriate measure mu has been introduced in G. The consequences of the formulation are analyzed in detail in the case where the measure mu is generated by a continuous, Markovian stochastic process. The calculation of the hysteresis properties of the ensemble is reduced to the solution of the level-crossing problem for the stochastic process. In particular, it is shown that, when the process is translationally invariant (homogeneous), the ensuing hysteresis properties can be exactly described by the Preisach model of hysteresis, and the associated Preisach distribution is expressed in closed analytic form in terms of the drift and diffusion parameters of the Markovian process. Possible applications of the formulation are suggested, concerning the interpretation of magnetic hysteresis due to domain wall motion in quenched-in disorder and the interpretation of critical state models of superconducting hysteresis.

Journal Article↗

Bilitranslocase is the protein responsible for the electrogenic movement of sulfobromophthalein in plasma membrane vesicles from rat liver: immunochemical evidence using mono- and poly-clonal antibodies.

Monoclonal antibodies raised against bilitranslocase, may display either inhibitory or enhancing activity on the electrogenic transport of sulfobromophthalein, evoked in rat liver plasma-membrane vesicles by the addition of valinomycin in the presence of K+. In both cases, the target protein is identified with a 37 kDa band in SDS-mercaptoethanol gel electrophoresis of solubilized membranes. The electrophoretically homogeneous protein isolated by ion-exchange chromatography, corresponds in all respects to the 37 kDa protein band of bilitranslocase, obtained in the past by different techniques. Using this protein as antigen, a polyclonal monospecific antibody preparation has been obtained. As expected, the antibody preparation inhibits the electrogenic movement of sulfobromophthalein in plasma membrane vesicles from rat liver. It is concluded that the 37 kDa protein of bilitranslocase is at least a necessary component of the transport system involved in the sulfobromophthalein movement in plasma membrane.

Animals↗