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Concentration-dependent reversible self-oligomerization of serum albumins through intermolecular β-sheet formation.

Langmuir, 2014
Proteins inside a cell remain in highly crowded environments, and this often affects their structure and activity. However, most of the earlier studies involving serum albumins were performed under dilute conditions, which lack biological relevance.
Arpan Bhattacharya   +3 more
semanticscholar   +1 more source

Albumin Naskapi: A New Variant of Serum Albumin

Science, 1966
An apparently new variant of human serum albumin, albumin Naskapi, has been found in high frequency in the Naskapi Indians of Quebec and, in lower frequency, in other North American Indians. The family and population data of the albumin are consistent with its inheritance as a simple autosomal trait controlled by a gene designated
B. S. Blumberg, Liisa Melartin
openaire   +3 more sources

Differences between Urinary Albumin and Serum Albumin

Nature, 1962
IN the work reported here, the molecular size and the peptide patterns of the albumins found in normal urine were compared with those of serum albumin.
Ezio Merler   +3 more
openaire   +3 more sources

Copper(II) complexes of salicylaldehydes and 2-hydroxyphenones: synthesis, structure, thermal decomposition study and interaction with calf-thymus DNA and albumins

, 2015
The neutral mononuclear copper(II) complexes with substituted salicylaldehyde (X-saloH), or 2-hydroxyphenone (ketoH) ligands, having the formula [Cu(L)2(S)n] (where S = solvent CH3OH or H2O and n = 0, 1 or 2) have been prepared and characterized, and ...
Ariadni Zianna   +3 more
semanticscholar   +1 more source

Binding Properties of Glycosylated Albumin and Acetaldehyde Albumin

Alcoholism: Clinical and Experimental Research, 1985
Glucose and acetaldehyde react covalently with albumin to form the post‐translationally modified group of proteins, the glycosylated albumins and the acetaldehyde albumins, respectively. This study contrasts the binding ability of a major acetaldehyde albumin fraction synthesized in vitro with glycosylated albumin.
Alex F. Robertson   +3 more
openaire   +3 more sources

Hydrophobicity alone can not trigger aggregation in protonated mammalian serum albumins.

Physical Chemistry, Chemical Physics - PCCP, 2014
Amyloid fibrils are associated with neurodegenerative disorders and are formed by a number of proteins. In this study, the amyloid-forming behavior of several different serum albumins was examined at pH 3.5 i.e., about two pH units below their ...
J. M. Khan   +4 more
semanticscholar   +1 more source

Albumin and Glycated Albumin

1995
Serum albumin is a single polypeptide chain protein of 66 000 Da molecular weight without associated carbohydrate. Glycation of albumin can be induced by prolonged exposure to elevated blood glucose levels, analogous to the induction of glycated haemoglobin.
openaire   +2 more sources

The distribution of albumin precursor protein and albumin in liver

Biochemical and Biophysical Research Communications, 1976
Abstract Two different proteins precipitable with antiserum to albumin exist in liver. One is albumin, the other is precursor albumin. Liver cells in suspension contain mainly precursor, but secrete only albumin. In subcellular fractions isolated from liver homogenate, 95.3% of anti-albumin precipitable protein in the rough endoplasmic reticulum, 51 ...
Kaylene Edwards   +4 more
openaire   +3 more sources

Albumin Polymorphism (Albumin Naskapi) in Eskimos and Navajos

Nature, 1968
WE have described two polymorphic variants of serum albumin (Fig. 1). Of these, albumin Naskapi the electrophoretic mobility of which is greater than that of the usual albumin (albumin A) is relatively common in several North American Indian tribes. It has been identified in sera from Indians of the Naskapi, Montagnais, Sioux, Northern Athabascan and ...
Liisa Melartin   +2 more
openaire   +3 more sources

Study of single and double chain surfactant–cobalt(III) complexes and their hydrophobicity, micelle formation, interaction with serum albumins and antibacterial activities

, 2014
To develop surfactant based metallodrugs, it is important to know the role of the tail part of the surfactant–metal complexes in their hydrophobicity, micellization behaviour, interaction with biomacromolecules and cell penetration. Here, we have taken a
S. Veeralakshmi   +4 more
semanticscholar   +1 more source

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