PubMed · 4679986
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
D Genov, A Astrug, G Gizov, N Popov, S Iordanova. 1972. [Immunochemical studies in diffuse nephropathy].. https://pubmed.ncbi.nlm.nih.gov/4679986/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Explore the source record for details and available documents.
Electrophoretic mobilities, mu, of nine proteins (M(r) 14,200 to 70,000) in 28 mM Tris/47 mM glycine buffer at pH 8.77 and 5 mM ionic strength were measured by laser Doppler velocimetry and correlated to ratios of charge (q) to molecular weight (M(r)) and shape factor (f/f0) by the equation mu(f/f0) = (Aq/Mpr-B). This correlation was previously reported for peptides and proteins for mu measured at 100 mM ionic strength. When A = 6.048 x 10(-3), B = 1.13 x 10(-5), and p = 2/3, the correlation fitted 51 measured and literature values over the molecular weight range of 178 to 140,000 for components whose electrophoretic mobilities ranged from +13.35 x 10(-5) to -19.7 x 10(-5) cm2/(V.s). The experimental measurements confirm the general suitability of p = 2/3 and show that the familiar charge/mass relation for electrophoresis is applicable to proteins in low-ionic-strength buffers which are typical of electrochromatography systems. Extrapolation of the correlation to different ionic strengths indicates that a low-ionic-strength buffer amplifies differences of electrophoretic mobility as a function of charge/mass, while high ionic strength diminishes such differences.
beta-Galactosidase can be assayed by monitoring the generation of the fluorescent products, fluorescein-mono-beta-D-galactopyranoside and fluorescein, when the fluorogenic substrate fluorescein-di-beta-D-galactopyranoside is used. We have used capillary electrophoresis with ultrasensitive laser-induced fluorescence detection to monitor the formation of the fluorescent products of off-column enzymatic reactions. By analyzing as little as 40 pl of the enzymatic mixture we obtain limits of detection of 6.5 x 10(-14) M beta-galactosidase or 1.6 molecules based on the detection of fluorescein-mono-beta-D-galactopyranoside.