Serum free 5-methoxypsoralen fraction in health and psoriasis: relationship with human serum albumin concentration

1993 ◽  
Vol 285 (5) ◽  
pp. 287-290 ◽  
Author(s):  
P. Muret ◽  
P. Humbert ◽  
S. Makki ◽  
P. Bechtel ◽  
S. Urien ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Albumin Concentration ◽  
Serum Albumin Concentration ◽  
Serum Free ◽  
Human Serum Albumin Concentration

Measurement of human serum albumin concentration using Raman spectroscopy setup

2016 ◽  
Vol 48 (6) ◽  
Author(s):  
Dmitry N. Artemyev ◽  
Valery P. Zakharov ◽  
Igor L. Davydkin ◽  
Julia A. Khristoforova ◽  
Anastasia A. Lykina ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Albumin Concentration ◽  
Serum Albumin Concentration ◽  
Human Serum Albumin Concentration

Fortification of blood plasma from cancer patients with human serum albumin decreases the concentration of cisplatin-derived toxic hydrolysis products in vitro

Metallomics ◽  
2014 ◽  
Vol 6 (11) ◽  
pp. 2034-2041 ◽  
Author(s):  
Thomas T. Morris ◽  
Yibing Ruan ◽  
Victor A. Lewis ◽  
Aru Narendran ◽  
Jürgen Gailer
Keyword(s):  
Side Effects ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Cancer Patients ◽  
Albumin Concentration ◽  
Serum Albumin Concentration ◽  
Hydrolysis Products ◽  
Human Serum Albumin Concentration

Boosting the human serum albumin concentration in cancer patients is suggested to be a feasible strategy to possibly reduce the severe toxic side-effects of cisplatin.

A rapid paper-based detection system for determination of human serum albumin concentration

2018 ◽  
Vol 352 ◽  
pp. 241-246 ◽  
Author(s):  
Ruey-Jen Yang ◽  
Chin-Chung Tseng ◽  
Wei-Jhong Ju ◽  
Hsiang-Li Wang ◽  
Lung-Ming Fu
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Detection System ◽  
Albumin Concentration ◽  
Serum Albumin Concentration ◽  
Human Serum Albumin Concentration

scholarly journals 1723. Human Serum Albumin Regulates the Growth of Candida auris in vitro

2019 ◽  
Vol 6 (Supplement_2) ◽  
pp. S631-S632
Author(s):  
Jun Sakai
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Candida Species ◽  
Blood Protein ◽  
Albumin Concentration ◽  
Blood Proteins ◽  
Candida Auris ◽  
Xtt Assay ◽  
High Albumin

Abstract Background Candida auris is commonly detected in human ear secretions. However, C. auris occasionally causes bloodstream infections even in immunocompetent patients resulting in poor prognosis. It was speculated that C. auris growth within the blood might be regulated by proteins in the bloodstream. Thus, in this study, the potential role of blood proteins in the regulation of C. auris growth was investigated. Methods Five Candida species (C. albicans, C. auris, C. glabrata, C. parapsilosis, and C. tropicalis) were incubated overnight. Colony suspensions for each species were prepared and adjusted to OD 1.0 at absorbance 0.1. Then, human serum albumin (HSA) and bovine serum albumin (BSA) were diluted (2.5 g/dL–0.002 g/dL) and mixed with the suspensions. Mixed samples were adjusted to 100 μL and incubated on MHA plates at 35°C for 2 days. Then, 50 μL of the combined sample was extracted and streaked onto Yeast extract-Peptone-Dextrose (YPD) agar. The remaining 50 μL sample was analyzed using an XTT assay. Further testing was then conducted on the effects of a specific blood protein albumin on Candida. Thereby, C. albicans and C. auris were cultured following the procedure above and stained with Annexin V and PI. Results The growth of C. auris mixed with a high albumin concentration (2.5~0.15 g/dL) was regulated compared with that of other Candida species (P < 0.01) (Figures 1 and 2); however, the growth of C. auris mixed with a lower albumin concentration was similar to that of other species. The wash-out study showed that C. auris growth and survival in the high albumin concentration was not different than that of other species. Conclusion HSA and BSA regulated C. auris growth which led to increased necrosis of C. auris. Conversely, growth of the other Candida species was not regulated. Therefore, albumin might be involved in the growth and necrosis of C. auris. As the highest concentration at which albumin regulated C. auris growth was similar to that found in human serum, it is possible that serum albumin might help prevent C. auris from entering the bloodstream via the ear or skin. Disclosures All authors: No reported disclosures.

Investigation of relaxation times in 5-fluorouracil and human serum albumin mixtures

2019 ◽  
Vol 44 (4) ◽  
pp. 524-529 ◽  
Author(s):  
Sibel Korunur ◽  
Bilgin Zengin ◽  
Ali Yilmaz
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Relaxation Times ◽  
Solution Temperature ◽  
Cancer Drug ◽  
Human Blood Plasma ◽  
Albumin Concentration ◽  
Protein Drug ◽  
Relaxation Rates

Abstract Background Human serum albumin (HSA) is often selected as a subject of any study because albumin is the most abundant protein in human blood plasma. NMR is recognized as a valuable method to determine the structure of proteins-ligand and protein-drug complexes. Objective – Aim of the study In this study, protein drug interactions were investigated using 5-Fluorouracil anti-cancer drug and human serum albumin protein. Materials and methods In this context 400 MHz NMR spectrometry was used and NMR relaxation rates in drug-albumin complex were investigated with respect to increase albumin concentration and increase in 5-Fluorouracil (5-FU)-albumin solution temperature. Results The results of this study indicated that 5-FU had a weak association with albumin, and it easily dissociated from the protein to which it was attached. Conclusion The obtained results also gave us useful information about molecular dynamics of drug-albumin interactions.

scholarly journals Investigating the Interaction of Nanodiamonds with Human Serum Albumin and Induced Cytotoxicity

2019 ◽  
Vol 2019 ◽  
pp. 1-9 ◽  
Author(s):  
Miaomiao Chen ◽  
Xiaoshuang Zuo ◽  
Qinqin Xu ◽  
Rong Wang ◽  
Suhua Fan ◽  
...  
Keyword(s):  
Cell Culture ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Biomedical Applications ◽  
Culture Medium ◽  
Cell Culture Medium ◽  
Serum Free Medium ◽  
Free Medium ◽  
Serum Free

Nanodiamonds (NDs) have been recognized as emerging carbon-based delivery vehicles due to their biocompatibility. NDs were reported to be nontoxic and suited for biomedical applications in the complete cell culture medium. However, in this study, the cytotoxicity of NDs in serum-free medium was studied and indicated that serum proteins in cell culture medium played significant effect on the toxicity of NDs. Therefore, the interaction mechanism between NDs and a serum protein (human serum albumin, HSA) was first investigated by fluorescence quenching technique and circular dichroism (CD) spectrometry. The results suggest that HSA strongly bonds on the NDs surface to form “protein corona,” which not only prevents the aggregation of NDs and improves its stability but also inhibits the cytotoxicity of NDs. In serum-free medium, NDs exhibited obvious toxicity toward the human lung epithelial cell line (BEAS-2B) and showed concentration-dependent cytotoxicity. In the presence of bovine serum albumin (BSA), which shares structural homology and similar properties with HSA, toxicity of NDs was apparently inhibited. Therefore, the interaction between serum protein and NDs should be considered in the understanding of the biological effects of NDs exposure in biomedical applications.

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