Results 151 to 160 of about 2,585,632 (205)
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Journal of Protein Chemistry, 1986
A theory is presented on the solubility of proteins, in the hydrated as well as in the dry state, and in water as well as in organic solvents. To this effect, colloidal stability is assimilated with the solubility of the proteins, considered as hydrated entities. By means of a surface thermodynamic approach it can be shown that an increase in size of a
C. J. van Oss +2 more
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A theory is presented on the solubility of proteins, in the hydrated as well as in the dry state, and in water as well as in organic solvents. To this effect, colloidal stability is assimilated with the solubility of the proteins, considered as hydrated entities. By means of a surface thermodynamic approach it can be shown that an increase in size of a
C. J. van Oss +2 more
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Interaction of soluble proteins with protein monolayers
Journal of the American Oil Chemists' Society, 1968AbstractThe direction and strength of intermolecular forces at an air‐water or oil‐water interface is such that many proteins in the interface are distorted in structure. This involves substantial changes in solubility and cross‐sectional area. Many of the changes can be accounted for by rupture of the secondary and tertiary bonds and are often ...
J D, Arnold, C Y, Pak
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Measuring and Increasing Protein Solubility
Journal of Pharmaceutical Sciences, 2008High concentration protein delivery is difficult to achieve for several protein pharmaceuticals due to low solubility. In this review, we discuss different types of low protein solubility, including low in vitro solubility, which is relevant to the formulation of protein pharmaceuticals. We also discuss different methods of measuring protein solubility
Saul R, Trevino +2 more
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Effect of carbohydrate on protein solubility
Archives of Biochemistry and Biophysics, 1983The effect of covalently attached carbohydrate on the solubility of a number of proteins has been examined by the PEG precipitation technique. Both increases and decreases in solubility are observed depending on the state of glycosylation, the type of protein, and temperature.
E Q, Lawson +5 more
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On protein solubility in organic solvent
Biotechnology and Bioengineering, 1994AbstractSolubility of a model protein, hen egg‐white lysozyme, was investigated in a wide range of neat nonaqueous solvents and binary mixtures thereof. All solvents that are protic, very hydrophilic, and polar readily dissolve more than 10 mg/mL of lysozyme (lyophilized from aqueous solution of pH 6.0).
J T, Chin, S L, Wheeler, A M, Klibanov
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Soluble Proteins in Thyroid Neoplasia
The Journal of Clinical Endocrinology & Metabolism, 1968ABSTRACT Soluble proteins were prepared from 36 thyroid tumors, 7 adenomas and 29 carcinomas, and studied by analytical ultracentrifugation and paper electrophoresis. Thyroglobulin-type proteins (thyroglobulin 19S, its dissociation product 12S and its polymers) were present only in tumors capable of accumulation and organisation of iodine either at the
L, Valenta +3 more
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Solubility of alkanes in protein solutions
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1967Abstract 1. 1. The solubility of homologous alkanes in solutions of different proteins was studied. The alkanes employed were pentane, heptane, nonane, and mixtures of pentane and nonane. The proteins were bovine serum albumin, β-lactoglobulin, chicken ovomucoid, and chicken ovalbumin.
A, Mohammadzadeh +3 more
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2019
Protein solubility determines the conditions under which the protein will remain in solution. As a result, it is an important quantity in applications that involve concentrated protein solutions. Here I describe the solubility measurement of the protein thaumatin in the presence of tartrate ions as a function of temperature.
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Protein solubility determines the conditions under which the protein will remain in solution. As a result, it is an important quantity in applications that involve concentrated protein solutions. Here I describe the solubility measurement of the protein thaumatin in the presence of tartrate ions as a function of temperature.
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Soluble proteins in chemosensory organs of phasmids
Insect Biochemistry and Molecular Biology, 1996Soluble proteins of low molecular weight have been purified from chemosensory organs of five species of Phasmids. On the basis of their N-terminal amino acid sequences, two classes can be identified. Polypeptides of 14 and 15 kDa, expressed in the antennae and legs of Eurycantha calcarata and Extatosoma tiaratum, as well as in the antennae of Carausius
Marina Mameli +4 more
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Soluble NSF-attachment proteins
The International Journal of Biochemistry & Cell Biology, 1998Soluble NSF-attachment proteins (SNAPs) are highly conserved proteins that participate in intracellular membrane fusion and vesicular trafficking. In mammals, there are three different isoforms of SNAPs, alpha-, beta- and gamma-SNAP. alpha- and gamma-SNAP are ubiquitously expressed, whereas beta-SNAP is the brain-specific isoform.
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