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R Borsali

Publications and source records attributed to R Borsali.

5 recordsLinked to original sources

Ultrastructural aspects of phytoglycogen from cryo-transmission electron microscopy and quasi-elastic light scattering data.

Phytoglycogen particles extracted from the sugary maize mutant su 1 and dispersed in water were studied using transmission electron microscopy (TEM) and light scattering. Dried specimens were either negatively stained with uranyl acetate or shadowed with W/Ta. Frozen-hydrated unstained particles embedded in a thin film of vitreous ice were also observed using cryo-TEM. The particles exhibited a spheroidal shape, with a diameter ranging from 30 to 100 nm. Some of them presented a multilobular morphology and appeared to be formed by smaller subunits, 20-30 nm in diameter, resembling the described beta-particles for animal glycogen. The diameter of stained and ice-embedded particles was measured from electron micrographs. The corresponding size distribution histograms showed that the average weight diameter of ice-embedded particles was higher than that of stained ones. In the latter case, a shrinkage of the particle was believed to occur during the drying process. Light scattering experiments confirmed the diameter of ice-embedded particles and indicated that they could be considered as uniformly dense spheroidal objects.

Cryoelectron Microscopy↗

Dynamic light scattering study of the two-domain structure of Humicola insolens endoglucanase V.

Endoglucanase V (EG V) of HUmicola insolens is composed of a catalytic domain and of a cellulose-binding domain linked by a 33 amino acid long peptide rich in Ser, Thr and Pro residues. This work describes the dynamic behavior of the two-domain structure of EG V as revealed by quasi-elastic light scattering experiments. For both the full-length and the isolated catalytic domain, the autocorrelation function is essentially described by a single relaxation mode. The equivalent hydrodynamic radius of the catalytic domain was found to correspond precisely to the dimensions measured from the previously determined three-dimensional structure. The results obtained with the full-length protein allow a description of the two domain structure of EG V similar to that resulting from earlier studies using small angle X-ray scattering on cellulases from Trichoderma reesei. The hydrodynamic dimensions of the entire enzyme can be approximated as an ellipsoid with dimensions of 42 x 133.6 A.

Binding Sites↗

[ECG compression method by using multiple polynomial modelling: comparison with wavelet-changing technique].

The proposed ECG compression combined two approaches, ECG beat alignment and polynomial modeling. QRS complexes are firstly detected then aligned in order to reduce high frequency changes from beat to beat. These changes are modeled by means a polynomial projection. ECG from MIT-BIH database are used to evaluate the performances of the proposed technique. A comparison with the wavelet approach is performed by means the compression ratio (CR) versus the RRD curve.

Algorithms↗