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1.
Phys Rev E ; 95(1-1): 013309, 2017 Jan.
Article in English | MEDLINE | ID: mdl-28208470

ABSTRACT

In this work, a hybrid lattice Boltzmann method (HLBM) is proposed, where the standard lattice Boltzmann implementation based on the Bhatnagar-Gross-Krook (LBGK) approximation is combined together with an unstructured finite-volume lattice Boltzmann model. The method is constructed on an overlapping grid system, which allows the coexistence of a uniform lattice nodes spacing and a coordinate-free lattice structure. The natural adaptivity of the hybrid grid system makes the method particularly suitable to handle problems involving complex geometries. Moreover, the provided scheme ensures a high-accuracy solution near walls, given the capability of the unstructured submodel of achieving the desired level of refinement in a very flexible way. For these reasons, the HLBM represents a prospective tool for solving multiscale problems. The proposed method is here applied to the benchmark problem of a two-dimensional flow past a circular cylinder for a wide range of Reynolds numbers and its numerical performances are measured and compared with the standard LBGK ones.

2.
Mol Cell Biochem ; 11(2): 97-101, 1976 Apr 28.
Article in English | MEDLINE | ID: mdl-1272258

ABSTRACT

Cytoplasmic aspartate aminotransferase from beef kidney loses 25% of its activity on nitration with tetranitromethane while the apoenzyme about 95%. In the holoenzyme 0.5 tyrosine residue and 1.0 tyrosine residue in the apoenzyme are nitrated per enzyme protomer. In addition 1 cysteine residue per protomer is oxidized in both. The presence of substrates, alpha-ketoglutarate and glutamate, both at ten times their Km values, does not change these results. Mercaptoethanol does not affect the residual activity of either the nitrated holo or apoenzyme. Dithionite abolishes the activity of the nitrated holoenzyme by reducing tha coenzyme moiety. It has no effect on the native holoenzyme or on either the native or nitroapoenzyme.


Subject(s)
Aspartate Aminotransferases/metabolism , Kidney/enzymology , Mitochondria/enzymology , Animals , Apoenzymes , Binding Sites , Cattle , Dithionite/pharmacology , Kinetics , Mercaptoethanol/pharmacology , Mercuribenzoates/pharmacology , Molecular Weight , Protein Binding , Protein Conformation , Spectrophotometry , Spectrophotometry, Ultraviolet , Tetranitromethane/pharmacology , Tyrosine/analysis
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