Soluble complexes of gum, aranbic with α-lactalbumin, and β-lactoglobulin above the protein isoelectric point: Analysis in terms of charge patches

2007 ◽  
pp. 329-336
Author(s):  
Renko de Vries
Keyword(s):  
Isoelectric Point ◽  
Point Analysis ◽  
Β Lactoglobulin ◽  
Soluble Complexes

Dynamics of the ceramic ultrafiltration of model proteins with different isoelectric point: Comparison of β-lactoglobulin and lysozyme

2007 ◽  
Vol 57 (2) ◽  
pp. 314-320 ◽  
Author(s):  
Rubén Ibáñez ◽  
M. Carmen Almécija ◽  
Antonio Guadix ◽  
Emilia M. Guadix
Keyword(s):  
Isoelectric Point ◽  
Β Lactoglobulin

Pressure dissociation of β-lactoglobulin oligomers near their isoelectric point

Soft Matter ◽  
2012 ◽  
Vol 8 (46) ◽  
pp. 11654 ◽  
Author(s):  
Ronald Gebhardt ◽  
José Toro-Sierra ◽  
Ulrich Kulozik
Keyword(s):  
Isoelectric Point ◽  
Β Lactoglobulin

scholarly journals Structural, functional, and idiotypic characteristics of a phosphorylcholine-binding IgA myeloma protein of C57BL/ka allotype.

1975 ◽  
Vol 141 (3) ◽  
pp. 608-619 ◽  
Author(s):  
J L Claflin ◽  
S Rudikoff ◽  
M Potter ◽  
J M Davie
Keyword(s):  
Amino Acids ◽  
Sequence Analysis ◽  
Binding Site ◽  
Isoelectric Point ◽  
Light Chain ◽  
Hypervariable Region ◽  
Myeloma Protein ◽  
Heavy Chains ◽  
Point Analysis

An IgA phosphorylcholine (PC)-binding myeloma protein with IgCH allotypic determinants different from those of BALB/c mice is characterized. The myeloma, CBPC 2, was induced in the CB-20 strain of mice which is congenic to BALB/c but differs from it by carrying the A15 allotypic determinant of C57BL/ka mice. Sequence analysis of the CBPC 2 light chain through the first hypervariable region, as well as isoelectric point analysis, show that this chain is indistinguishable from that of T15, a PC-binding myeloma protein of BALB/c origin. The heavy chains of CBPC 2 and T15 differ by only two amino acids (positions 14 and 16) through the first hypervariable region. As measured by inhibition of precipitation, both CBPC 2 and T15 have the same specificity for PC, glycerophosphorylcholine, acetylcholine, and choline. In addition, CBPC 2 possesses the binding site-associated idiotypic determinant which is present on T15. However, like normal or induced C57BL/6 anti-PC antibody, it does not possess the nonbinding site idiotypic determinant.

point-Analysis Using the Extrapolation Method in the Analytical Electron microscope

1990 ◽  
Vol 48 (2) ◽  
pp. 430-431
Author(s):  
Zenji Horita ◽  
Ryuzo Nishimachi ◽  
Takeshi Sano ◽  
Minoru Nemoto
Keyword(s):  
Electron Microscope ◽  
Extrapolation Method ◽  
X Ray ◽  
Absorption Correction ◽  
Point Analysis ◽  
Analytical Electron ◽  
Analytical Electron Microscope ◽  
Data Points ◽  
Identical Composition ◽  
X Ray Absorption

Absorption correction is often required in quantitative x-ray microanalysis of thin specimens using the analytical electron microscope. For such correction, it is convenient to use the extrapolation method[l] because the thickness, density and mass absorption coefficient are not necessary in the method. The characteristic x-ray intensities measured for the analysis are only requirement for the absorption correction. However, to achieve extrapolation, it is imperative to obtain data points more than two at different thicknesses in the identical composition. Thus, the method encounters difficulty in analyzing a region equivalent to beam size or the specimen with uniform thickness. The purpose of this study is to modify the method so that extrapolation becomes feasible in such limited conditions. Applicability of the new form is examined by using a standard sample and then it is applied to quantification of phases in a Ni-Al-W ternary alloy.The earlier equation for the extrapolation method was formulated based on the facts that the magnitude of x-ray absorption increases with increasing thickness and that the intensity of a characteristic x-ray exhibiting negligible absorption in the specimen is used as a measure of thickness.

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