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Human serum albumin

About: Human serum albumin is a research topic. Over the lifetime, 9402 publications have been published within this topic receiving 269029 citations. The topic is also known as: serum albumin & ALB.


Papers
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Journal ArticleDOI
TL;DR: The new genre of green nanoparticles exhibit remarkable Protein Tyrosine Phosphatase 1B (PTP 1B) inhibitory activity and in vitro stability in various physiological medium including saline, histidine, cysteine, bovine serum albumin (BSA), human serumalbumin (HSA) and buffers (pH 5, 7 and 9).

70 citations

Journal ArticleDOI
TL;DR: The structural alterations in the HSA after binding to the taurine were demonstrated by exploiting various biophysical techniques and molecular docking study deciphered the possible residues involved in protein and drug interaction.

70 citations

Journal ArticleDOI
TL;DR: The H-D exchange in aqueous solutions of defatted human serum albumin (HSA) has been investigated by the infrared spectroscopic technique and the relaxation spectrum may be taken as an illustration of the distribution of changes in free energy of the transitions of the protein, exposing the peptide groups to the solvent.

70 citations

Journal ArticleDOI
TL;DR: In this article, the authors investigated the mutual interactions between three differently substituted B-ring hydroxyl groups (Pelargonidin-3-O-glucoside, P3G, C3G and D3G) and human serum albumin (HSA) under physiological pH conditions.

70 citations

Journal ArticleDOI
TL;DR: This study suggests that Arg-gingipains and, to a lesser extent, Lys-gingIPain play an important role in the growth of P. gingivalis in a defined medium containing a human protein as the sole carbon and nitrogen source.
Abstract: Porphyromonas gingivalis, a bacterium associated with active chronic periodontitis lesions, produces several proteolytic enzymes that are thought to be involved in host colonization, perturbation of the immune system, and tissue destruction. The aim of the present study was to investigate the contribution of Arg- and Lys-gingipains produced by P. gingivalis to its growth. Although all of the proteins studied were degraded by P. gingivalis, only human serum albumin and transferrin supported growth during serial transfers in a chemically defined medium (CDM). Growth studies with site-directed gingipain-deficient mutants of P. gingivalis revealed that inactivation of both gingipains prevents growth, whereas inactivation of either Arg- or Lys-gingipain activity extended the doubling times to 33 or 13 h, respectively, compared to 9 h for the parent strain. Growth of the mutants and the parent strain was similar when the CDM was supplemented with a protein hydrolysate instead of human serum albumin. Incubation of resting P. gingivalis ATCC 33277 cells with fluorophore-labeled albumin indicated that the proteolytic fragments generated by the gingipains were internalized by the bacterial cells. Internalization of fluorophore-labeled albumin fragments was reduced or completely inhibited in the proteinase-deficient mutants. Interestingly, gingival crevicular fluid samples from diseased periodontal sites contained low-molecular-mass albumin fragments, whereas samples from healthy sites did not. The critical role of proteinases in the growth of P. gingivalis was further investigated using specific Arg- and Lys-gingipain inhibitors. Adding the inhibitors to CDM containing albumin revealed that leupeptin (Arg-gingipain A and B inhibitor) was more efficient at inhibiting growth than cathepsin B inhibitor II (Lys-gingipain inhibitor). Our study suggests that Arg-gingipains and, to a lesser extent, Lys-gingipain play an important role in the growth of P. gingivalis in a defined medium containing a human protein as the sole carbon and nitrogen source.

70 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023174
2022423
2021284
2020333
2019333
2018337