Serum Albumin

Peters, Theodore

doi:10.1016/s0065-3233(08)60065-0

Cited by 2,260 publications

(1,200 citation statements)

References 299 publications

Supporting

Mentioning

1,115

Contrasting

Unclassified

Order By: Relevance

“…It appears to be a connecting segment between the second and third domains. Enzymatic cleavage of undenatured human serum albumin occurs after positions 380, 387, and 389 (25), indicating that the end of domain 2 is exposed. In general, amino acid replacements are more readily tolerated at the surface of a protein; for example, nearly all substitutions on the surface of the hemoglobin molecule are harmless (26).…”

Section: Sugita Et Al (21) Had Reported That the Molecular Abnormalitymentioning

confidence: 99%

Point substitutions in Japanese alloalbumins.

Arai

Madison²,

Huss³

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

We have completed the structural study of five rare types of inherited albumin variants (alloalbumins) discovered in the Biochemical Genetics Study of 15,581 unrelated children in Hiroshima and Nagasaki. We have also identified the structural chane inl five other alloalbumin specimens detected during clinical electrophoresis of sera from Japanese living near Tokyo. Each of the five albumin variants from Nagasaki and Hiroshima has a single amino acid substitution. AlU of these substitutions differ, and none has been reported in non-Japanese populations. No instances of proalbumin variants or of albumin B (the most frequent alloalbumins in Caucasians) were detected in the children in Hiroshima and Nagasaki. However, one instance of a variant proalbumin and two examples of albumin B occurred in Japanese from the vicinity of Tokyo. In addition a previously unreported point substitution was found in albumin Tochigi, which is present in two unrelated persons from Tochigi prefecture. Four of the point mutations in the Japanese alloalbumins are in close proximity in a short segment of the polypeptide chain (residues 354-382) in which three additional point substitutions have been reported in diverse populations. These results, combined with earlier data, suggest that point substitutions are grouped in certain segments of the albumin molecule.

show abstract

Section: Sugita Et Al (21) Had Reported That the Molecular Abnormalitymentioning

confidence: 99%

Point substitutions in Japanese alloalbumins.

Arai

Madison²,

Huss³

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…It comprises a single chain with 585 amino acids organized in three similar domains (I, II, and III), each consisting of two subdomains (IA, IB, etc.). The principal regions of ligand binding sites of albumin are located in hydrophobic cavities in subdomains IIA and IIIA (sites I and II) [23][24][25]. A typical site marker for site I is the anticoagulant drug warfarin (WF) [26][27][28][29], while dansylglycine (DG) shows specificity for site II (see Fig.…”

Section: Introductionmentioning

confidence: 99%

Characterization of the binding sites of the anticancer ruthenium(III) complexes KP1019 and KP1339 on human serum albumin via competition studies

et al. 2012

View full text Add to dashboard Cite

Indazolium trans-[tetrachloridobis(1H-indazole)ruthenate(III)] (KP1019) and its Na + analogue (KP1339) are two of the most prominent non-platinum antitumor metal complexes currently undergoing clinical trials. After intravenous administration, they are known to bind to human serum albumin (HSA) in a non-covalent manner. In order to elucidate their HSA binding sites, displacement reactions with the established site markers warfarin and dansylglycine as well as bilirubin were monitored by spectrofluorimetry, ultrafiltration−UV-vis spectrophotometry and/or capillary zone electrophoresis. Conditional stability constants for the binding of KP1019 and KP1339 to sites I and II of HSA were determined, indicating that both Ru(III) compounds bind into both sites with moderately to strong affinity (logK 1 ' = 5.3-5.8). No preference for either binding site was found and similar results were obtained for both metal complexes, demonstrating low influence of the counter ion on the binding event.

show abstract

“…Albumin is the major protein in human serum and the most significant protein found in the extracellular fluid compartment (5).…”

Section: Introductionmentioning

confidence: 99%

The Utility of the Serum Albumin Levels on Admission for Predicting Angiographic No Reflow After Primary Percutaneous Coronary Intervention in Patients With ST-Segment Elevation Myocardial Infarction

Acet¹,

Ertaş²,

Aydın³

et al. 2015

Turk J Bioch

View full text Add to dashboard Cite

Amaç: Düşük serum albümin (SA) düzeyleri artmış kardiyovasküler mortalite ile ilişkilidir. Bazal SA seviyelerinin primer perkütan koroner girişim (p-PKG) yapılan hastalarda akışsızlık fenomeni ile ilgili olup olmadığını araştırdık. Yöntem: Geriye dönük olarak p-PKG ile tedavi edilen ST yükselmeli myokard infarktüsü (STYMI)'lı 358 hasta alındı. Hasta takibi hastaneiçi dönemde yapıldı. Önceki çalışmalara uygun olarak, TIMI akım derecesi ≤2, TIMI akım derecesi >3 olanlarda ise MBG <2 olanlar akışsızlık fenomeni olarak değerlendirildi. Hastalar başvuru SA düzeylerine göre iki gruba ayrıldı. SA <3,5 g/dl olanlar hipoalbüminemik grup ve SA düzey > 3,5 g/dl yüksek albüminemik grup olarak değerlendirildi. Bulgular: PKG yapılan toplam 358 (yaş 62±14 yaş, % 72 erkek) hasta alındı. Başvuru SA düzeyleri akışsızlık fenomeni olan grupta normal akım olan gruba göre anlamlı bir şekilde daha düşüktü (p=0,021). Sonuç: Başvuru SA seviyeleri akut STYMI hastalarda p-PKG sonrası-akışsızlık fenomeninin gelişimini tahmin edebilir. Başvuru hipoalbüminemili hastalar kötü klinik ve anjiyografik sonuçları ile ilgilidir ve STYMI p-PKG ile tedavi edilen hastalarda hastane içi mortalite ve pulmoner ödem ve kardiyojenik şok gelişimi tahmin edilebilmektedir.Objective: Low serum albumin (SA) levels are associated with increased cardiovascular mortality. We investigated whether baseline SA levels are associated with no-reflow in patients undergoing primary percutaneous coronary intervention (p-PCI). Method: STEMI patients treated by p-PCI were included in the study. The patients were followed during in hospital period. We defined angiographic no-reflow phenomenon as a coronary TIMI flow grade ≤2 after vessel re-canalized or TIMI flow grade 3 together with a final MBG < 2, in the same manner as was adopted in previous studies. The patients were divided into two groups according to the SA levels on admission, that is hypoalbuminemia group was SA<3.5 g/dl and high albuminemia group SA level was >3.5 g/dl. Results: A total of 358 patients (aged 62+14 years; 72% men) who underwent p-PCI were enrolled in the study. Admission SA levels were significantly lower in the noreflow group than in the normal-reflow group (p=0.021) Conclusion: Admission SA levels may predict the development of no-reflow phenomenon after p-PCI in patients with acute STEMI. Hypoalbuminemia on admission is related to worse clinical and angiographic outcomes and predicts inhospital mortality and development of advanced pulmonary edema and cardiogenic shock (higher Killip class) in patients treated with p-PCI for STEMI.Anahtar Kelimeler: Serum albumin düzeyi, Akışsızlık fenomeni, Perkütan koroner girişim, Akut myokard infarktüsü.

show abstract

Serum Albumin

Cited by 2,260 publications

References 299 publications

Point substitutions in Japanese alloalbumins.

Point substitutions in Japanese alloalbumins.

Characterization of the binding sites of the anticancer ruthenium(III) complexes KP1019 and KP1339 on human serum albumin via competition studies

The Utility of the Serum Albumin Levels on Admission for Predicting Angiographic No Reflow After Primary Percutaneous Coronary Intervention in Patients With ST-Segment Elevation Myocardial Infarction

Contact Info

Product

Resources

About