University of North Florida
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Stuart Chalk, Ph.D.
Department of Chemistry
University of North Florida
Phone: 1-904-620-1938
Fax: 1-904-620-3535
Email: schalk@unf.edu
Website: @unf

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β-Lactoglobulin

@ ChemSpider@ NIST@ PubChem

Citations 4

"Further Studies On The Reaction Of Amines And Proteins With 4-fluoro-7-nitrobenzofurazan"
Anal. Chim. Acta 1985 Volume 170, Issue 1 Pages 81-87
Hiroshi Miyano, Toshimasa Toyo'oka and Kazuhiro Imai

Abstract: The reaction of glycine with the title compound (NBD-F) was investigated to establish conditions that provide a high formation rate of the fluorescent adduct NBD-glycine and a low hydrolysis rate of the reagent. The effects of temp., organic solvents and buffer solution are reported. Conditions are given for derivatizing both low-mol.-wt. amines and proteins with NBD-F after HPLC separation. For low-mol.-wt. amines, acetonitrile is preferred to ethanol as reaction solvent, in the presence of borate buffer of pH 8 to 8.5. For proteins (separated by size-exclusion chromatography), water (e.g., 50%) should be present for sensitive reaction. Detection limits for human serum albumin, β-lactoglobulin and myoglobin are 6.6 pmol, 8.4 pmol and 11 pmol, respectively; these are larger than the limits of u.v. detection at 210 nm, but fluorescence detection may have advantages in selectivity.
Serum Human HPLC Spectrophotometry Post-column derivatization

"Flow Injection Determination Of Proteins Based On The Lowry Spectrophotometric Method"
Anal. Chim. Acta 1989 Volume 217, Issue 2 Pages 359-362
Hans Lüdi and Anita Bärtschi

Abstract: The flow injection system was based on the use of Folin - Ciocalteu reagent, with 1,4-dithio-DL-threitol to accelerate the formation of the colored complex, which was detected at 700 nm. The calibration graph for bovine serum albumin was rectilinear between 0.01 and 0.1 mg mL-1. The detection limit was 5 µg mL-1 and up to 0.5 mg mL-1 could be determined. The injection frequency was 20 h-1. Results obtained by the flow injection method and by the manual Lowry procedure correlated well. Egg lysozyme, alkaline phosphatase and β-lactoglobulin were also determined.
Egg Cow Serum Spectrophotometry Complexation Method comparison

"Some Observations On The Automation By Flow Injection Analysis Of The Spectrophotometric Determination Of Amino-acids And Proteins With Phthalaldehyde"
Microchim. Acta 1992 Volume 108, Issue 3-6 Pages 293-298
M. J. Medina Hernández, S. Sagrado Vives and M. C. García Alvarez-Coque

Abstract: An improved flow injection system for the determination of total free amino-acids and protein is described. The procedure is based on the rapid reaction of α- and ε-amino-groups in amino-acids and proteins with phthalaldehyde in the presence of N-acetyl-L-cysteine at room temperature and pH 8.5 to 9.5. The absorbance due to the reaction products is monitored at 336 nm. For the determination of free amino-acids the system is calibrated with 0.5 to 9 mM leucine; the detection limit is 10 µM. For the determination of proteins the system is modified to include a longer reaction period. Calibration graphs are prepared with bovine serum albumin, casein and β-lactoglobulin over the range 2 to 20 µM; the detection limit is 1 µM.
Cow Serum Spectrophotometry Automation

"Characterization Of Proteins Separated By Displacement Chromatography Using Low-angle Laser-light-scattering Photometry"
Chromatographia 1994 Volume 38, Issue 5-6 Pages 349-354
R. Mhatre, R. Qian, I. S. Krull, S. Gadam, S. M. Cramer

Abstract: Displacement chromatography with low-angle laser-light-scattering (LALLS) photometric detection was used to measure the mol. wt. of β-lactoglobulin A and B. A feed solution (1 ml) containing 20 mg/ml of β-lactoglobulin in the mobile phase (75 mM Tris-HCl buffer of pH 7.5) was passed (0.1 ml/min) through a Protein-Pak Q-8HR anion-exchange column (10 cm x 5 mm i.d.); after 10 min, 7 mL of dextran sulfate displacer solution (20 mg/ml) was injected through a switching valve. A Thermo Separation Products model KMX-6 LALLS photometer and a UV detector (310 nm) were used for the online measurement of the mol. wt. Both forms of the analyte were eluted as dimers, and LALLS photometry was able to detect these and also their impurities. The mol. wt. of the proteins were 6-8% higher than the theoretical value for a dimer, and the presence of aggregates was indicated by LALLS photometry, but not by the UV signal. Comparative studies were also carried out by size-exclusion chromatography and FIA before LALLS and UV detection, and the results are reported.
HPIC Spectrophotometry Method comparison