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Serum albumin

About: Serum albumin is a(n) research topic. Over the lifetime, 16337 publication(s) have been published within this topic receiving 516395 citation(s). The topic is also known as: blood albumin & ANALBA.


Papers
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Journal ArticleDOI
16 Jul 1992-Nature
TL;DR: The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 Å and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serumalbumin.
Abstract: The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 A. It comprises three homologous domains that assemble to form a heart-shaped molecule. Each domain is a product of two subdomains that possess common structural motifs. The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. The structure explains numerous physical phenomena and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serum albumin.

3,273 citations

Journal ArticleDOI
TL;DR: The results by this method agree very well with those obtained by electrophoresis and salt fractionation and the method is simple, it has excellent precision and the reagents are stable.
Abstract: A rapid and reliable method for measuring serum albumin employing bromcresol green is described. The addition of albumin to a solution of bromcresol green in a 0.075 M succinate buffer pH 4.20 results in an increase in absorbance at 628 nm. The absorbance-concentration relationship is linear for samples containing up to 6 g/dl albumin. Bilirubin, moderate lipemia, and salicylate do not interfere with the analysis. The use of nonionic surfactant (Brij-35) reduces the absorbance of the blank, prevents turbidity and provides linearity. The results by this method agree very well with those obtained by electrophoresis and salt fractionation. The method is simple, it has excellent precision and the reagents are stable. A protein standard is introduced which can be employed for both the total serum proteins and albumin determinations.

3,175 citations

Journal ArticleDOI
TL;DR: The Lowry protein assay is a sensitive but highly nonspecific procedure that has been modified so that protein can be assayed in the presence of interfering chemicals.
Abstract: The Lowry protein assay is a sensitive but highly nonspecific procedure. The standard Lowry protein assay has been modified so that protein can be assayed in the presence of interfering chemicals. The method is based on the observation that in the presence of 125 μg/ml of Na-deoxycholate, bovine serum albumin (5—50 μg) is reproducibly precipitated (90–104%) by 6% trichloroacetic acid. Interference by sucrose, glycerol, Tris—HCl, Tricine, and EDTA can be eliminated. Protein samples containing carrier ampholytes can also be assayed provided their NaCl concentration is adjusted to 1 m .

3,099 citations

Book ChapterDOI
TL;DR: This chapter provides an insight of the findings of past significant papers with the current knowledge of the recently determined high resolution X-ray structure of serum albumin and suggests that AFP may have a higher affinity for some unknown ligands important for fetal development.
Abstract: Publisher Summary This chapter provides an insight of the findings of past significant papers with the current knowledge of the recently determined high resolution X-ray structure of serum albumin. The most outstanding property of albumin is its ability to bind reversibly an incredible variety of ligands. The sequences of all albumins are characterized by a unique arrangement of disulfide double loops that repeat as a series of triplets. Albumin belongs to a multigene family of proteins that includes α- fetoprotein (AFP) and vitamin D-binding protein (VDP), also known as G complement (Gc) protein. Although AFP is considered the fetal counterpart of albumin, its binding properties are distinct and it is suggested that AFP may have a higher affinity for some unknown ligands important for fetal development. Domain structure and the arrangement of the disulfides, the surface charge distribution, and the conformational flexibility of the albumin molecule are described. The nature of ligand binding, including small organics, long-chain fatty acids, and metals, to multiple sites on the albumin molecule is clearly depicted. The chapter concludes with the perceptive comments on future directions being taken to explore the structure and function of this fascinating protein.

2,847 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20221
2021263
2020296
2019295
2018323
2017330