Results 221 to 230 of about 52,375 (251)

Altered chain-length and glycosylation modify the pharmacokinetics of human serum albumin

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2009
Human serum albumin with modified plasma half-life will be useful for clinical purposes. Therefore, the pharmacokinetics of three of each of the following types of genetic variants, and of their corresponding normal albumin, were examined in mice: N-terminally elongated, C-terminally truncated and glycosylated albumins.
Iwao, Yasunori, Hiraike, Mikako, Kragh-Hansen, Ulrich, Kawai, Keiichi, Suenaga, Ayaka, Maruyama, Toru, Otagiri, Masaki   +6 more
openaire   +3 more sources

Therapeutic in vivo synthetic chemistry using an artificial metalloenzyme with glycosylated human serum albumin

2022
The concept of "therapeutic in vivo synthetic chemistry" refers to chemical synthesis in living systems using new-to-nature reactions for the treatment or diagnosis of diseases. This review summarizes our development of therapeutic in vivo synthetic chemistry using glycan-modified human serum albumin (glycoHSA) and utilizing the selective glycan ...
Kenshiro, Yamada, Kyohei, Muguruma, Katsunori, Tanaka   +2 more
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Effects of nonenzymatic glycosylation and fatty acids on tryptophan binding to human serum albumin

Biochemical Pharmacology, 1992
The effects of bound fatty acids and nonenzymatic glycosylation (NEG) on tryptophan binding to human serum albumin (HSA) were examined utilizing a rate of dialysis technique. HSA with 0, 1, 2, 3, or 5 mol of palmitate bound per mol of HSA was glycosylated in vitro to a level exceeding that seen in diabetes.
J P, Bohney, R C, Feldhoff
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Interaction of glycosylated amino acids with human serum albumin

1999
The nonenzymatic interaction of glucose with amino groups of proteins and amino acids results in generation of stable products. This post-translational nonenzymatic modification of proteins and amino acids is called glycosylation [1]. The glycosylation occurs due to a small fraction of glucose (about 0.002% of the total amount) which is in the opened ...
I. I. Stepuro, N. A. Chaikovskaya
openaire   +1 more source

Microheterogeneity of serum glycosyl albumin in diabetes mellitus.

Diabete & metabolisme, 1985
Proteins purified by affinity chromatography on Blue-Sepharose CL-6B from serum of 10 normal controls and 19 Type I diabetic patients were studied by means of combined ultrathin isoelectric focusing and photochemical silver stain. While only a single band of protein (characterized as albumin by crossed immunoelectrophoresis) with a pI of 4.7 was found ...
G M, Ghiggeri, G, Candiano, G, Delfino, G, Pallavicini, C, Queirolo   +4 more
openaire   +1 more source

[Bilirubin binding to glycosylated human serum albumin].

Voprosy meditsinskoi khimii, 1987
Glycosylation of human blood serum albumin was carried out by means of prolonged incubation of the protein with an excess of D-glucose or D-glucose-6-phosphate. The amount of glucose covalently bound to the protein was determined using thiobarbituric acid or pyridoxal-5-phosphate.
I I, Stepurovo, A A, Solodunov, N V, Iaroshevich   +2 more
openaire   +1 more source

[Adducts of glycosylated serum albumin with amino acids].

Ukrainskii biokhimicheskii zhurnal (1978), 1986
Glycosylation of human serum albumin was conducted by its long incubation with the excess either of D-glucose or D-glucose-6-phosphate at 37 degrees C. The glycosylated fractions were isolated by the cation-exchange chromatography on CM-cellulose. The quantity of glucose bound covalently with protein was determined by thiobarbituric acid.
I I, Stepuro, T P, Piletskaia, N A, Iaroshevich, A V, Naumov   +3 more
openaire   +1 more source

Synthesis and characterization of glycosylated nitrogen mustard derivatives and their interaction with bovine serum albumin

Research on Chemical Intermediates, 2012
To improve the specificity of nitrogen mustards towards tumor cells, glucose-nitrogen mustard, fructose-nitrogen mustard, and lactose-nitrogen mustard were prepared as three novel glycosylated nitrogen mustard derivatives by esterification of bis(2-chloroethyl)carbamic chloride (BCC) with glucose, fructose, and lactose, respectively.
Shan Li, He-ping Li, Long Qin
openaire   +1 more source

Evaluation of the effect of phenylpropanoids on the binding of heparin to human serum albumin and glycosylated human serum albumin concerning anticoagulant activity: A comparison study

International Journal of Biological Macromolecules
The nonenzymatic advanced glycation end products (AGEs) and the accumulation of AGEs are the two main factors associated with the long-term pathogenesis of diabetes. Human serum albumin (HSA) as the most abundant serum protein has a higher fortuity to be modified by nonenzymatic glycation.
Vali, Akbari, Sirous, Ghobadi
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Effect of Nonenzymatic Glycosylation on the Magnetic Resonance Imaging (MRI) Contrast Agent Binding to Human Serum Albumin

Journal of Medicinal Chemistry, 2012
Enhanced nonenzymatic glycosylation (NEG) of human serum albumin (HSA) is observed in diabetic patients. This modifies some of the physiological functions of HSA, as the binding of ligands. Some gadolinium complexes, commonly used as MRI contrast agents, have a high affinity for HSA, which enhances their efficacy.
Henoumont, Céline, Laurent, Sophie, Muller, Robert, Vander Elst, Luce   +3 more
openaire   +3 more sources