نتایج جستجو برای: human serum albumin

تعداد نتایج: 1897664  

Journal: :The Journal of clinical investigation 1961
D GITLIN K SCHMID D P EARLE H GIVERLBER

An unusual serum protein anomaly, the occurrence of two electrophoretically distinct albumins in the same serum, was recently reported by Knedel (2, 3) who observed the abnormality in eight members of two different families and termed the condition "double-albuminemia." A similar anomaly was found by Earle, Hutt, Schmid and Gitlin in 25 of 43 individuals in a single family (4, 5), and additiona...

Journal: :biomacromolecular journal 0
elham mozaffari department of chemistry, gorgan branch, islamic azad university, gorgan, iran elham tazikeh-lemeski department of chemistry-gorgon branch-islamic ad university-gorgan-iran ali akbar saboury institute of biochemistry and biophysics, university of tehran, tehran, iran

human serum albumin (hsa) is the most abundant protein in the blood plasma. drug binding to hsa is crucial to study the absorption, distribution, metabolism, efficiency and bioavailability of drug molecules. in this study, isothermal titration calorimetry and molecular dynamics simulation of hsa and its complex with indometacin (im) were performed to investigate thermodynamics parameters and th...

2013
MILTON TABACHNICK

In previous work from this laboratory (1) studies on equilibrium dialysis were carried out to determine the binding constants for the interaction of human serum albumin with thyroxine and its analogs. The classical technique of equilibrium dialysis as described by Scatchard and others (2-6) was employed. At present it seems clear that thyroxine in human serum migrates to at least three differen...

2003
GERALD A. BALLOU PAUL D. BOYER JAMES MURRAY LUCK FUNSTON G. LUM

The present studies were designed to develop a rapid micromethod for investigation of the effects of heat on relatively concentrated solutions of human serum albumin. The method so devised is proposed for the routine study of commercial preparations, and for inquiry into some of the factors that appear to determine the thermal stability of an albumin solution. As will be clear from the paragrap...

Journal: :Clinica chimica acta; international journal of clinical chemistry 2013
Jeanethe Anguizola Ryan Matsuda Omar S Barnaby K S Hoy Chunling Wa Erin DeBolt Michelle Koke David S Hage

Glycation involves the non-enzymatic addition of reducing sugars and/or their reactive degradation products to amine groups on proteins. This process is promoted by the presence of elevated blood glucose concentrations in diabetes and occurs with various proteins that include human serum albumin (HSA). This review examines work that has been conducted in the study and analysis of glycated HSA. ...

2015
Miklós Poór Beáta Lemli Mónika Bálint Csaba Hetényi Nikolett Sali Tamás Kőszegi Sándor Kunsági-Máté HJ (Ine) van der Fels-Klerx

Citrinin (CIT) is a mycotoxin produced by several Aspergillus, Penicillium, and Monascus species. CIT occurs worldwide in different foods and drinks and causes health problems for humans and animals. Human serum albumin (HSA) is the most abundant plasma protein in human circulation. Albumin forms stable complexes with many drugs and xenobiotics; therefore, HSA commonly plays important role in t...

2003
Arthur H. Thomas

Thyroxine and triiodothyronine are transported in the blood as noncovalent complexes with certain serum proteins. This has been shown by many investigators and was the subject of an extensive recent review by Robbins and Rall (1). The binding proteins are an a-globulin (called thyroxine-binding globulin), a prealbumin, and serum albumin. The first appears to be the most significant binder of th...

Journal: :The Journal of biological chemistry 1961
G L TRITSCH C E RATHKE N E TRITSCH C M WEISS

Thyroxine and triiodothyronine are transported in the blood as noncovalent complexes with certain serum proteins. This has been shown by many investigators and was the subject of an extensive recent review by Robbins and Rall (1). The binding proteins are an a-globulin (called thyroxine-binding globulin), a prealbumin, and serum albumin. The first appears to be the most significant binder of th...

Journal: :The Journal of biological chemistry 1976
C C Kuenzle N Gitzelmann-Cumarasamy K J Wilson

A label for the bilirubin binding sites of human serum albumin was synthesized by reacting 2 mol of Woodward's reagent K (N-ethyl-5-phenylisoxazolium-3'-sulfonate) with 1 mol of bilirubin. This yielded a water-soluble derivative in which both carboxyl groups of bilirubin were converted to reactive enol esters. Covalent labeling was achieved by reacting the label with human serum albumin under n...

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