Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
Polish version English version Language
enabled [disable] Abstract
Number of results

Results found: 4

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

Search:
in the keywords:  albumin
help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
1
Content available remote

Interaction of anthracene and its oxidative derivatives with human serum albumin

100%
Skupińska K., Zylm M., Misiewicz I., Kasprzycka-Guttman T.
Acta Biochimica Polonica
|
2006
|
vol. 53
|
issue 1
101-112
EN
Binding affinities of ten polycyclic aromatic hydrocarbons to albumin were determined: anthracene, its eight oxy-derivatives: anthraquinone, 9-anthracenemethanol, 9-anthraldehyde, 9-anthracenecarboxylic acid, 1,4-dihydroxyanthraquinone, 1,5-dihydroxyanthraquinone, 1,8-dihydroxyanthraquinone, 2,6-dihydroxyanthraquinone and benzo[a]pyrene. The quenching of albumin fluorescence was used to measure the PAH - protein interaction. The theoretical curve of calculated fluorescence was fitted to experimental data after necessary corrections regarding PAHs fluorescence and inner filter effect. From the numerical fitting the final association constants were calculated. Anthracene and anthraquinone failed to quench the albumin fluorescence. 9-anthracenecarboxylic acid showed the highest, while 9-anthracenemethanol the weakest albumin binding affinity. The affinity constants determined for 9-anthraldehyde and benzo[a]pyrene were of the same magnitude and indicated low-affinity binding to albumin. The constants obtained for the four dihydroxyanthraquinones were higher, but dissimilar, which suggests that the position of the functional group in anthracene molecule influences the binding constant. Moreover, this study suggests that the type of substituent plays a significant role in PAH-albumin complex formation. The carboxylic group increases the binding affinity of the anthracene molecule the most rather than the presence of both carbonyl and hydroxyl groups. The lowest affinity constants were obtained for aldehyde, methyl and carbonyl substituents.
2
Publication available in full text mode
Content available

The 30-day mortality predictor role of c-reactive protein/albumin ratio in critically ill COPD patients

100%
Cırık M. Ö., Baldemir R., Doğanay G. E., Ünver M., Avcı S.
|
XX
INTRODUCTION: Chronic Obstructive Pulmonary Disease (COPD) is a progressive disease that develops due to inflammation in the airways. The aim of this study is to demonstrate the effectiveness of c-reactive protein/albumin ratio (CAR) as a 30-day mortality indicator in COPD patients admitted to ICU. MATERIAL AND METHODS: A total of 235 COPD patients with available data between January 2018 and December 2018 were included in this retrospective cohort study. Demographics, APACHE II, Charlson comorbidity index (CCI), SOFA score, CAR and outcomes were evaluated. RESULTS: 87 (37%) of the cases were female and 148 (63%) were male. Their ages ranged from 26 to 95 years, with an average of 70.9± 11.4. The non-survivors had significantly higher APACHE II, CCI, SOFA score, procalcitonin, creatinine, mechanical ventilation (MV) time, WBC, CRP and CAR compared to the survivors (p˂0.05). Albumin and prealbumin were significantly lower (p˂0.05) in non-survivors. In the univariate model; age, sepsis, inotropic support, APACHE II score, CCI, SOFA, procalcitonin, creatinine, MV time, WBC, CRP, albumin, prealbumin and CAR were observed to be significantly effective (p˂0.05) in predicting 30-day mortality. In the multivariate reduced model; inotropic support, SOFA, WBC and prealbumin value exhibited significant independent (p<0.05) effectiveness in predicting 30-day mortality. Albumin, CRP, CAR, APACHE II, SOFA and CCI value were observed to be significant in predicting mortality (p=0.000). CONCLUSIONS: In the study, the predictive power of APACHE II score, CCI, SOFA score, albumin and prealbumin values alone was found to be significantly higher than that of the CAR.
3
Publication available in full text mode
Content available

Evaluation of plasma concentrations of selected antioxidant parameters in patients with active Crohn’s disease

75%
Szczeklik K., Krzyściak W., Cibor D., Kozioł K., Pocztar H., Pytko-Polończyk J., Mach T., Owczarek D.
Folia Medica Cracoviensia
|
2018
|
vol. 58
|
issue 2
4
Publication available in full text mode
Content available

Quercetin influences BSA alpha-helical structures of native, ACR- and NaNO2-modified BSAs

75%
Rorbach-Dolata A., Żurawska-Płaksej E., Piwowar A.
Acta Poloniae Pharmaceutica - Drug Research
|
2018
|
vol. 75
|
issue 6
1339-1346
EN
Quercetin (QUE) is a plant flavonoid with a multifarious spectrum of properties. It is a prominent component of the human diet, considered to be safe and beneficial for human health. Acrylamide (ACR) and sodium nitrate III (NaNO2) are also present in the diet and may demonstrate adverse and toxic effects on the macromolecules and tissues of the human organism. Albumin, the most abundant blood protein, is the most susceptible to the action of various exogenous factors, which may lead to structural damage and functional disturbances. The aim of this study was to estimate ACR- and NaNO2-induced changes in the secondary structure of bovine serum albumin (BSA), using circular dichroism (CD), and to determine the impact of quercetin on these modifications. BSA was incubated with ACR and NaNO2 solutions in the absence and presence of QUE in two different concentrations (3 mM and 500 µM), and changes in albumin alpha-helical structure were determined by CD. BSA secondary structure was vulnerable to alterations upon treatment with acrylamide and NaNO2, as well as quercetin. QUE, depending on concentration and incubation time, caused a decrease of around 13-19% in the alpha-helix content of BSA molecules, but also prevented the changes in the protein alpha-helical structure initiated by ACR and NaNO2. The most spectacular inhibition was revealed for QUE in lower concentrations after 24h of incubation with NaNO2. Although QUE reveals protective effect towards albumin modifications, it is difficult to unambiguously define whether this effect is advantageous, because quercetin itself causes alterations in BSA structure.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.