Results 151 to 160 of about 69,876 (195)

Isoelectric points of proteins: A table

Analytical Biochemistry, 1978
We have prepared a table of isoelectric points (pZ) of proteins selected from the literature. Initially, we retrieved a computerized bibliography from the MEDLARS data base covering the time period of January 1970-March 1976. This search, supplemented by an additional search of Biological Abstracts, produced about 3000 citations. From this bibliography
D, Malamud, J W, Drysdale
openaire   +2 more sources

The isoelectric point of Cypridina luciferase

Archives of Biochemistry and Biophysics, 1955
Abstract Measurements of the mobility of Cypridina luciferase by means of paper electrophoresis at seven pH values between 2.38 and 6.18 indicate an apparent isoelectric point of 3.28. The reliability of this value is enhanced by the close agreement found between the isoelectric point of bovine plasma albumin determined by paper electrophoresis and
J H, WEIR, F I, TSUJI, A M, CHASE
openaire   +2 more sources

Isoelectric focusing and isoelectric points of bovine liver histones

Analytical Biochemistry, 1980
Abstract A technique for isoelectric focusing of total histones in very narrow pH gradients is described. The isoelectric focusing was performed in 5% acrylamide gels at the pH range 9–11 in long quartz tubes (24 cm) in a nitrogen atmosphere. The total bovine liver histones separated into five main fractions which were identified as H1, H3, H2B, H2A,
K H, Valkonen, R S, Piha
openaire   +2 more sources

Expression and purification of a recombinant avidin with a lowered isoelectric point in Pichia pastoris [PDF]

Protein Expression and Purification, 2003
A recombinant glycosylated avidin (recGAvi) with an acidic isoelectric point was expressed and secreted by the methylotrophic yeast Pichia pastoris. The coding sequence for recGAvi was de novo synthesized based on the codon usage of P. pastoris.
Thomas R Ward
exaly   +2 more sources

Method for Estimation of Protein Isoelectric Point

Analytical Chemistry, 2012
Adsorption of sample protein to Eu(3+) chelate-labeled nanoparticles is the basis of the developed noncompetitive and homogeneous method for the estimation of the protein isoelectric point (pI). The lanthanide ion of the nanoparticle surface-conjugated Eu(3+) chelate is dissociated at a low pH, therefore decreasing the luminescence signal.
Pihlasalo, Sari, Auranen, Laura, Hänninen, Pekka, Härmä, Harri   +3 more
openaire   +3 more sources

The isoelectric point of BaTiO3

Journal of the European Ceramic Society, 2000
Abstract The value of the isoelectric point (IEP) of BaTiO 3 is highly significant for the development of a fully rational basis for the successful processing of BaTiO 3 powder by aqueous routes. We report here experimental evidence that the true IEP value for BaTiO 3 is in the neutral pH range (6–7).
M.C. Blanco López, B. Rand, F.L. Riley
openaire   +1 more source

Determination of the isoelectric point of proteins by capillary isoelectric focusing

Journal of Chromatography A, 2004
Different ways of determining isoelectric points (pI) of proteins in capillary isoelectric focusing are reviewed here. Due to the impossibility of direct pH measurements in the liquid phase, such assessments have to rely on the use of pI markers. Different types of pI markers have been described: dyes, fluorescently labelled peptides, sets of proteins ...
openaire   +2 more sources

Isoelectric points of proteins: Theoretical determination

Analytical Biochemistry, 1989
Three methods for calculating the isoelectric points (pI) of proteins, provided that their amino acid compositions are known, are described. The comprehensive and abridged procedures involve solutions of polynomial equations of different degrees depending on whether pK values of the specific acid-base residues or the means of some of those values ...
A, Sillero, J M, Ribeiro
openaire   +2 more sources

Pressure Stability of Proteins at their Isoelectric Points

Protein & Peptide Letters, 2004
Yeast alcohol dehydrogenase is slowly denatured at moderate hydrostatic pressure (t(1/2) approximately equals 30 min at 2 kbar and pH 7). The extent of denaturation is pH dependent with maximal stability near the isoelectric point of the protein, pH = 5.4.
Gene, Kidman, Hyun, Park, Dexter B, Northrop   +2 more
openaire   +2 more sources

Cross Partition and Isoelectric Points of Proteins

Nature, 1970
AQUEOUS mixtures of dextran and polyethylene glycol give rise to liquid two-phase systems suitable for the partition of proteins1–5. The partition behaviour of proteins depends to a great extent on the ionic composition of the phase system and on the charge of the protein. Negatively charged materials, for example, have higher partition coefficients in
P A, Albertsson, S, Sasakawa, H, Walter
openaire   +2 more sources