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legumin/arnold-chiari malformation
Povezava se shrani v odložišče
3 rezultatov
Changes of the oligomeric structure of legumin from pea (Pisum sativum L.) after succinylation.
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Prijava / prijava
The influence of various levels of succinylation on the structure of the legumin from pea seed has been studied by the techniques of sedimentation velocity, viscometry, fluorescence and circular dichroism spectroscopy, as well as dynamic light scattering. The protein dissociates gradually into the
Physico-chemical characterization of legumin-T from faba bean (Vicia faba L).
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Prijava / prijava
Legumin-T, the high-molecular mass product of limited tryptic hydrolysis of faba bean legumin, was investigated using hydrodynamic methods, static light scattering, fluorescence and ultraviolet spectroscopy. The following physico-chemical parameters were determined in a high-ionic strength buffer
Shape, symmetry, hydration and secondary structure of the legumin from Vicia faba in solution.
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Prijava / prijava
The following physical parameters of the legumin from Vicia faba were determined by means of small-angle X-ray scattering, quasi-elastic light scattering and circular dichroism: molar mass, M = 3.5 X 10(5) g/mol; radius of gyration, Rg = 4.45 nm; maximum dimension, L = 13 nm; translational diffusion
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