0-Lactoglobulin analysis

Cheison, S. C., Schmitt, M., Leeb, E., Letzel, T., Kulozik, U. (2010). Influence of temperature and degree of hydrolysis peptide composition of trypsin hydrolysates of b-lactoglobulin Analysis by LC-ESI-TOE/MS. Food Chemistry, 121,451-461. 

Table 5.8 Polypeptides detected during the LC-electrospray-MS analysis of the tryptic digest from / -lactoglobulin (/ILG). Reprinted from 7. Chromatogr., A, 763, Tnrnla, V. E., Bishop, R. T., Ricker, R. D. and de Haseth, J. A., Complete structnre elncidation of a globular protein by particle beam hqnid chromatography-Fourier transform infrared spectrometry and electrospray hqnid chromatography-mass spectrometry - Seqnence and conformation of / -lactoglobulin , 91-103, Copyright (1997), with permission from Elsevier Science...

Hattori, T., Hallberg, R., Dubin, P.L. (2000). Roles of electrostatic interaction and polymer structure in the binding of p-lactoglobulin to anionic polyelectroytes measurement of binding constants by frontal analysis continuous capillary electrophoresis. Langmuir, 16, 9738-9743. 

Braunitzer, G., Chen, R., Schrank, B, and Stangl, A. 1972. Automatic sequential analysis of a protein (/3-lactoglobulin AB). Hoppe-Seyler s Z. Physiol. Chem. 353, 832-834 (German). 

Figure 8. Fast analysis of proteins. Column Hy-Tach micropellicular C-18 silica, 30x4.6mm eluent A, 0.1% (v/v) TFA in water, eluent B, 95% (v/v) ACN in water containing 0.1% (v/v) TFA flow rate, 4.0 ml/min. temp., 80°C. Initial column inlet pressure, 260 bars sample, 15 pi of a mixture containing =1 pg each of ribonuclease A (1), cytochrome C (2), lysozyme (3) and P-lactoglobulin A (4). Elution was carried out with a gradient 20 to 50% B in 0.5 min and return to starting conditions in 0.1 min. The dotted line represents gradient profile of ACN. The analysis was carried out with the house built protein analyzer described under Figure 7.

Jones, A.D., Tier, C.M., and Wilkins, J.P.G. 1998. Analysis of the Maillard reaction products of (3-lactoglobulin and lactose in skimmed milk powder by capillary electrophoresis and electrospray mass spectrometry. J. Chromatogr. 822, 147—154. 

Large sections of protein titration curves are often equally time-independent and reversible, as, for instance, the acid part of the titration curve of (3-lactoglobulin shown in Fig. 2. Any such section of the titration curve will again represent thermodynamic equilibrium and it may be subjected to thermodynamic analysis, as outlined in Sections VI and VII. 

The results of C-terminal sequence analysis on a 1 nmol sample of bovine beta-lactoglobulin A are shown in (Figure 5). The first three cycles of analysis show the identification of cycle-1 lie (I), cycle-2 His (H), and cycle-3 Cys (C), confirming the expected full-length protein sequence. The initial recovery of cycle-1 lie is approximately 40%. 

Benhamou and Guastalla (1960) were the first to question the assumption of irreversibility with an analysis of the adsorption of insulin, /3-lactoglobulin, and ribonuclease. They investigated whether the Gibbs adsorption equation was obeyed. This basic equation, applicable to reversible adsorption, is firmly based on thermodynamics and has been amply verified experimentally. It can be written in the simple form... 

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