Protein quantification by bicinchoninic acid (BCA) assay follows complex kinetics and can be performed at short incubation times

Cortés-Ríos, Javiera; Zárate, Alejandro; Figueroa, Juan David; Medina, Joaquı́n; Fuentes‐Lemus, Eduardo; Rodríguez-Fernández, María; Aliaga, Margarita E.; López-Alarcón, Camilo

doi:10.1016/j.ab.2020.113904

Cited by 67 publications

(38 citation statements)

References 35 publications

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“…The protein solubility of the samples (unheated and heated samples) were calculated by quantifying proteins before and after centrifugation. The protein content of the samples was determined using the bicinchoninic acid assay ( Cortés-Ríos et al, 2020 ). Briefly, sample (25 μL) was mixed with bicinchoninic acid (BCA) solution (200 μL) in a 96-well plate and placed in a plate reader (Biotek Instruments, Winooski, VT, USA) for 30 min at 37°C.…”

Section: Methodsmentioning

confidence: 99%

Effect of Modified Casein to Whey Protein Ratio on Dispersion Stability, Protein Quality and Body Composition in Rats

Jeong

Park

Kim

et al. 2021

Food Sci Anim Resour

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The present study was designed to investigate the effects of protein formula with different casein (C) to whey protein (W) ratios on dispersion stability, protein quality and body composition in rats. Modification of the casein to whey protein (CW) ratio affected the extent of protein aggregation, and heated CW-2:8 showed a significantly increased larger particle (>100 μm) size distribution. The largest protein aggregates were formed by whey protein self-aggregation. There were no significant differences in protein aggregation when the CW ratios changed from 10:0 to 5:5. Based on the protein quality assessment (CW-10:0, CW-8:2, CW-5:5, and CW-2:8) for four weeks, CW-10:0 showed a significantly higher feed intake (p<0.05), but the high proportion of whey protein in the diet (CW-5:5 and CW-2:8) increased the feed efficiency ratio, protein efficiency ratio, and net protein ratio compared to other groups. Similarly, CW-2:8 showed greater true digestibility compared to other groups. No significant differences in fat mass and lean mass analyzed by dual-energy x-ray absorptiometry were observed. A significant difference was found in the bone mineral density between the CW-10:0 and CW-2:8 groups (p<0.05), but no difference was observed among the other groups. Based on the results, CW-5:5 improved protein quality without causing protein instability problems in the dispersion.

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Section: Methodsmentioning

confidence: 99%

Effect of Modified Casein to Whey Protein Ratio on Dispersion Stability, Protein Quality and Body Composition in Rats

Jeong

Park

Kim

et al. 2021

Food Sci Anim Resour

View full text Add to dashboard Cite

show abstract

“…In theory, when making standard curve in colorimetric method, specific proteins and solvents should be adopted according to the corresponding sample compositions [58][59][60]. In some cases, though, a single standard curve was constructed for BCA testing on different protein solutions [61][62][63]. As for collagen and multiple extracting agents, this approach may affect the accuracy of protein concentration test.…”

Section: Resultsmentioning

confidence: 99%

A comparative study on the extraction effects of common agents on collagen-based binders in mural paintings

Zhu

Yang

et al. 2021

Herit Sci

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In this paper, a comparative study was conducted on the extraction effects of six agents for collagen-based mural painting binders. These agents were used to extract the residual proteins in the non-aged and thermal aged samples. The protein extraction efficiencies of different extracting agents were quantitatively determined by bicinchoninic acid (BCA) method, and then processed by multivariate analysis of variance (MANOVA). The impact of the extraction process on the protein structure was characterized by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), ultraviolet absorption spectrum (UV) and circular dichroism (CD). The results showed that, for both non-aged and aged samples, the extraction efficiency of 2 M guanidine hydrochloride (GuHCl) was significantly higher than the other five agents, with less damage to the protein structure during the extraction process.

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“…200 µL/well protein lysis RIPA buffer (89901, ThermoFisher Scientific, Waltham, USA) supplied with Protease Inhibitor (78442, ThermoFisher Scientific) was used for protein extraction. Protein concentrations in the cellular lysate were measured using Pierce T M BCA Protein Assay Kit (23225, ThermoFisher Scientific) [24]. Further, 20 µg protein samples per lane were separated using 10% SDS-PAGE gel by electrophoresis and transferred to a Nitrocellulose membrane.…”

Section: Western Blot Analysismentioning

confidence: 99%

Effect of Low-Level Er: YAG (2940 nm) laser irradiation on the photobiomodulation of mitogen-activated protein kinase cellular signaling pathway of rodent cementoblasts

Yong¹,

Li²,

Mizrahi³

et al. 2022

Front. Biosci. (Landmark Ed)

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Backgrounds: Dental avulsion due to trauma, especially in young patients, is a worldwide problem, requiring tooth replacement. Delayed replantation could cause tooth loss when the cementum is severely damaged. A small number of studies has reported that photobiomodulation (PBM) therapy using Er: YAG laser irradiation activates cellular signaling responses in different cell types, resulting in a variety of favorable biological effects. The aim of this in vitro study was to evaluate the potential biostimulatory effect of low-level Er: YAG laser irradiation on the biological responses of cultured mouse cementoblasts (OCCM-30), including the mitogen-activated protein kinases (MAPKs). Methods: OCCM-30 cells were exposed to 2940 nm Er: YAG laser irradiation for 15 s at 0.34 W (pulse duration of 100 or 1000 µs, 17 mJ/pulse) at energy densities of 1 or 2 J/cm 2 . Irradiated and non-irradiated OCCM-30 cells were tested for migration (Scratch assay), proliferation (MTS assay) and functional differentiation (Alizarin Red S assay). Lumican (Lum) and Fibromodulin (Fmod) gene expression, and activation of MAPKs, were assessed by RT-PCR and Western blotting, respectively. Results: Low-level Er: YAG laser irradiation at 2 J/cm 2 and pulse duration of 1000 µs resulted in the highest migration rate and proliferation. Moreover, the pulse duration irradiation of 100 µs increased Lum expression. Fmod expression was increased after 1000 µs pulse duration laser stimulation. Low-level Er: YAG laser irradiation increased the mineralization of OCCM-30 cells after 7 days and activated ERK1/2, P38 and JNK signaling. Conclusions: Low-level Er: YAG laser irradiation induces OCCM-30 cell migration, proliferation and differentiation, and activates the MAPK signaling pathway.

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Protein quantification by bicinchoninic acid (BCA) assay follows complex kinetics and can be performed at short incubation times

Cited by 67 publications

References 35 publications

Effect of Modified Casein to Whey Protein Ratio on Dispersion Stability, Protein Quality and Body Composition in Rats

Effect of Modified Casein to Whey Protein Ratio on Dispersion Stability, Protein Quality and Body Composition in Rats

A comparative study on the extraction effects of common agents on collagen-based binders in mural paintings

Effect of Low-Level Er: YAG (2940 nm) laser irradiation on the photobiomodulation of mitogen-activated protein kinase cellular signaling pathway of rodent cementoblasts

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