Albumin in patients with liver disease shows an altered conformation.

Paar M, Fengler VH, Rosenberg DJ, Krebs A, Stauber RE, Oettl K, Hammel M, Commun Biol 4(1):731 (2021) Europe PMC

SASDLC4 – Human Albumin (HSA) Healthy donor used for HNA1, HNA2, HMA fractions

MWexperimental 69 kDa
MWexpected 69 kDa
log I(s) 2.78×103 2.78×102 2.78×101 2.78×100
Albumin small angle scattering data  s, nm-1
ln I(s)
Albumin Guinier plot ln 2.79×103 Rg: 2.8 nm 0 (2.8 nm)-2 s2
Albumin Kratky plot 1.104 0 3 sRg
Dmax: 8.5 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Human Albumin (HSA) Healthy donor used for HNA1, HNA2, HMA fractions in 20 mM Tris, 150 mM KCl, 2% glycerol, pH 7.4 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS) storage ring (Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2.1 m and at a wavelength of λ = 0.1127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 55.00 μl sample at 5 mg/ml was injected at a 0.50 ml/min flow rate onto a Shodex KW-800 series column at 20°C. 600 successive 3 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   69.4 kDa
UniProt   P02768
Sequence   FASTA