Bradford protein assay

About: Bradford protein assay is a research topic. Over the lifetime, 635 publications have been published within this topic receiving 239107 citations.

Honey proteins and their interaction with polyphenols

Abstract: This project aimed to determine the protein profiles and concentration in honeys, effect of storage conditions on the protein content and the interaction between proteins and polyphenols. Thirteen honeys from different botanical origins were analyzed for their protein profiles using SDS-PAGE, protein concentration and phenolic content, using the Pierce Protein Assay and Folin-Ciocalteau methods, respectively. Protein-polyphenol interactions were analyzed by a combination of the extraction of honeys with solvents of different polarities followed by LCjMS analysis of the obtained fractions. Results demonstrated a different protein content in the tested honeys, with buckwheat honey possessing the highest protein concentration. We have shown that the reduction of proteins during honey storage was caused, partially, by the protein complexation with phenolics. The LCjMS analysis of the peak eluting at retention time of 10 to 14 min demonstrated that these phenolics included flavonoids such as Pinobanksin, Pinobanksin acetate, Apigenin, Kaemferol and Myricetin and also cinnamic acid.

Food protein: food colour interactions and its application in rapid protein assay.

Abstract: SaeedS�MG,�AbdullahSU,�SayeedSA,�AliR�(2010):�Food protein: Food colour interactions and its application in rapid protein assay CzechJ�FoodSci,�28:�506-513 Theuniformdistributionofcoloursasadditivesinamajorityofthefoodsystemsisareliableindicationthatoneor� morecomponentsoffoodsareabletobindwithcolourmoleculesandactastheircarriers �However, �thefoodcom- ponentsactingasthecolourcarriershavenotbeenidentified �Thepresentpaperdescribesthebindingcapacityof� Carmoisinewithavarietyoffoodproteins, �ourresultshaveshownthattheintensity, �staining, �andsharpnessofthe� stainedproteinbandswereexcellentascomparedtoCoomassieBrilliantBlueR�250,�whichisanestablishedstain - ingagentforvisualisingelectrophoreticallyresolvedproteins �ThedataillustratesthatCarmoisineisafastreacting� dyeformingcolour-complexeswithalltypesoffoodproteinsincludingcurryleavesproteins �Theproteinbandsare� visualisedwithinanhourwhichisusefulfortheinitialimmediateproteinidentifications�Theexperimentsrelatedto� thestainingoftheresolvedproteinswithCarmoisinehaveshownthatthedyeishighlysensitive, �rapid, �andlasting� Thefood-dyecanprovideaquickproteinassayasoftendesiredinresearchworks, �theresultsmaybelaterconfirmed� byusingCoomassieifsorequired �Inviewofitsstrongbindingwithalmostallproteins, �itwasthoughtthathuman� proteasespresentinthedigestivetractmaynothydrolysetheboundproteinscompletelyandmayrestricttheproteo - lyticdigestion �However, �theexperimentsbasedonthetrypticdigestibilityin vitro revealedthatcolourbindinghas� noadverseeffectonhydrolysisofpeptidebondsbytheintestinalproteases

Effects of extraction methods on protein properties obtained from paddy rice and germinated paddy rice.

Abstract: Rice protein has attracted considerable attention recently due to its physiological effects. This study extracted the proteins from paddy rice (PR) and germinated paddy rice (GPR) using three methods i.e., alkaline, sodium dodecyl sulfate (SDS) reagent and enzymatic extractions. The extracted proteins or protein fractions were assessed for their properties using various techniques. Data were analyzed by 2'3 factorial design experiment. It was found that germination and extraction methods significantly affected the concentration of protein fractions when analyzed by Bradford assay. Average protein fraction concentration of the GPR was lower than that of PR. SDS-PAGE patterns of protein fractions obtained from PR and GPR using any extraction method displayed similar protein profiles. Three major protein bands at about 13 kDa (prolamin), 22-23 kDa (basic glutelin) and 37-39 kDa (acidic glutelin) with small amount of 57 kDa proglutelin were observed. For amino acid profile, germination increased the content of most amino acids, resulting in the higher content of amino acids in GPR, excepted for some amino acids. When processed with in vitro digestion, protein fractions from GPR exhibited a higher level of digestibility than those from PR as evidenced by the less intensity of the protein bands obtained from SDS-PAGE. Alkaline and SDS reagent extractions provided more digestible protein fractions than enzymatic extraction. Extraction methods also influenced phase transition of protein fractions as investigated by a DSC. Alkaline extraction resulted in protein fractions with higher phase transition temperature than the other methods. For antioxidant capacity, extraction methods as well as germination significantly affected antioxidant capacity of the protein fractions. Enzymatic extraction provided protein fractions with the best antioxidant capacity.

Gene–protein correlation in single cells

Abstract: We present a novel methodology combining traditional fluorescent in situ hybridization with an in situ protein detection technology called proximity ligation assay. This method has potential to perform a detailed analysis of the relationship between gene status and corresponding protein expression in cells and tissues. We demonstrate that the fluorescent in situ gene protein assay methodology is capable of resolving gene and protein patterns simultaneously on a cell-by-cell basis.