Results 231 to 240 of about 52,375 (251)
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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
A genetic variant of human serum albumin (alloalbumin) exhibited atypical electrophoretic mobility and chromatographic behavior apparently because of the effect of a point substitution on the molecular conformation. Three forms of albumin were isolated by DEAE HPLC chromatography: normal albumin, and two variant forms V1 and V2. The point substitution (
Y, Sakamoto +7 more
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A genetic variant of human serum albumin (alloalbumin) exhibited atypical electrophoretic mobility and chromatographic behavior apparently because of the effect of a point substitution on the molecular conformation. Three forms of albumin were isolated by DEAE HPLC chromatography: normal albumin, and two variant forms V1 and V2. The point substitution (
Y, Sakamoto +7 more
openaire +2 more sources
Glycosylation of serum albumin in diabetic humans with osmolar and acid-base disorders.
Diabete & metabolisme, 1985The rate of nonenzymatic glycosylation of serum albumin was determined in 7 diabetic patients at the onset and during the recovery of an acute metabolic derangement as defined by hyperglycemia, hyperosmolality and metabolic acidosis of various degrees. Serum glycosyl albumin concentration (chemically determined) was decreased after 1 day in 5 patients (
G M, Ghiggeri +3 more
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Glycosylation of Human Serum Albumin Induced by Α-Dicarbonyl Compounds
SSRN Electronic Journal, 2023Jianmei Wu +4 more
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Analytical Chemistry
Human serum albumin (HSA), the most abundant plasma protein predominantly synthesized and secreted by the liver, harbors atypical N-glycosylation modifications at Asn68 and Asn123. Despite their potential biological relevance, the comprehensive characterization of these modifications remains limited.
Yueyue Li +6 more
openaire +2 more sources
Human serum albumin (HSA), the most abundant plasma protein predominantly synthesized and secreted by the liver, harbors atypical N-glycosylation modifications at Asn68 and Asn123. Despite their potential biological relevance, the comprehensive characterization of these modifications remains limited.
Yueyue Li +6 more
openaire +2 more sources
Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB), 2002
Glucose reacts with the amino groups of protein to form a Schiff base that rearranges to form a ketoamine adduct. These early products eventually undergo irreversible chemical modifications generating advanced glycation end products (AGES). We reacted various sugars and sugar phosphates with bovine serum albumin allowing the formation of Amadori and ...
S D, Sharma +3 more
openaire +1 more source
Glucose reacts with the amino groups of protein to form a Schiff base that rearranges to form a ketoamine adduct. These early products eventually undergo irreversible chemical modifications generating advanced glycation end products (AGES). We reacted various sugars and sugar phosphates with bovine serum albumin allowing the formation of Amadori and ...
S D, Sharma +3 more
openaire +1 more source
Structural characterization and stability of glycated bovine serum albumin-kaempferol nanocomplexes
Food Chemistry, 2023Run-Hui Ma, Zhi-Jing Ni, Kiran Thakur
exaly
Radioimmunoassay of glycosylated albumin with monoclonal antibody to glucitol-lysine
Clinica Chimica Acta, 1987Sadahito Shin +2 more
exaly
INCREASED PERMEABILITY OF HAMSTER MICROCIRCULATION TO GLYCOSYLATED ALBUMIN
Lancet, The, 1987T Sampietro +2 more
exaly