Coomassie Brilliant Blue-binding: a simple and effective method for the determination of water-insoluble protein surface hydrophobicity

2016 ◽  
Vol 8 (4) ◽  
pp. 790-795 ◽  
Author(s):  
Yungang Cao ◽  
Jing Zhao ◽  
Youling L. Xiong
Keyword(s):  
Surface Hydrophobicity ◽  
Fluorescence Method ◽  
Brilliant Blue ◽  
Insoluble Protein ◽  
Protein Surface ◽  
Coomassie Brilliant Blue ◽  
Protein Surface Hydrophobicity ◽  
Coomassie Brilliant

A novel Coomassie Brilliant Blue-binding method, which correlated well with the widely accepted ANS fluorescence method (R = 0.95), was developed to determine the surface hydrophobicity of water-insoluble proteins.

Total protein determined in human breast milk by use of coomassie brilliant blue and centrifugal analysis.

1989 ◽  
Vol 35 (10) ◽  
pp. 2127-2129 ◽  
Author(s):  
Y Bergqvist ◽  
L Karlsson ◽  
L Fohlin
Keyword(s):  
Breast Milk ◽  
Total Protein ◽  
Brilliant Blue ◽  
Human Breast Milk ◽  
Human Breast ◽  
Simple Method ◽  
Coomassie Brilliant Blue ◽  
Kjeldahl Method ◽  
Coomassie Brilliant

Abstract This simple method of centrifugal analysis for total protein in human breast milk is based on the change in the wavelength of the absorbance maximum of Coomassie Brilliant Blue G-250 when the dye is bound to protein. Within-run and between-day CVs were 3.8% and 4.8%, respectively. Compared with a micro-Kjeldahl method for determination of total nitrogen, the coefficient of correlation was 0.99.

scholarly journals Combined quantitative cytophotometric method for staining indolyl and sulfhydryl groups and protein.

1983 ◽  
Vol 31 (7) ◽  
pp. 967-970 ◽  
Author(s):  
Y Nakae ◽  
M Shono ◽  
H Ishizuka
Keyword(s):  
Sulfhydryl Groups ◽  
Brilliant Blue ◽  
Quantitative Histochemistry ◽  
Coomassie Brilliant Blue ◽  
Protein Staining ◽  
Coomassie Brilliant

Sulfenylation with 2-nitrophenylsulfenyl chloride (NPS-Cl), which is specific for tryptophyl and cysteinyl residues in protein, was applied to quantitative histochemistry. By measurement of the absorbance values at 370 nm of sections stained with NPS-Cl, Beer-Lambert's law was found to hold for NPS staining. Treatment of NPS-stained sections with 2-mercaptoethanol (ME) (NPS-ME staining) resulted in sulfenylation of tryptophyl residues only. For determination of the amounts of tryptophyl and cysteinyl residues per unit of protein, protein staining with Coomassie Brilliant Blue (CB) was combined with NPS and NPS-ME staining. CB and NPS-CBB staining also followed Beer-Lambert's law. By measuring the absorbance values at 370 and 650 nm of doubly stained sections, the relative contents of tryptophyl and cysteinyl residues in various tissue proteins were calculated. This method will be useful for the investigation of changes in both protein amount and composition.

Determination of Sepharose-bound protein with Coomassie brilliant blue G-250

1985 ◽  
Vol 151 (2) ◽  
pp. 571-574 ◽  
Author(s):  
R.A. Asryants ◽  
I.V. Duszenkova ◽  
N.K. Nagradova
Keyword(s):  
Brilliant Blue ◽  
Brilliant Blue G ◽  
Coomassie Brilliant Blue ◽  
Coomassie Brilliant

Comparison of Coomassie Brilliant Blue protein dye-binding assays for determination of urinary protein concentration.

1987 ◽  
Vol 33 (4) ◽  
pp. 577-578 ◽  
Author(s):  
T Marshall ◽  
K M Williams
Keyword(s):  
Protein Concentration ◽  
Urinary Protein ◽  
Brilliant Blue ◽  
Binding Assays ◽  
Coomassie Brilliant Blue ◽  
Standard Assay ◽  
Dye Binding ◽  
Coomassie Brilliant ◽  
Assay Protocol

Abstract We investigated the influence of assay protocol upon results of Coomassie Brilliant Blue protein dye-binding assays for urinary protein. Sensitivity and working range for, and linearity of response (including dilution dependence) of, three standard assays and four micro assays to bovine albumin, gamma-globulin, and urine are compared. The Read and Northcote standard assay (Anal Biochem 1981; 116:53-64) appears to be the method of choice.

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