THE BUOYANT BEHAVIOR OF BOVINE SERUM MERCAPTALBUMIN IN SALT SOLUTIONS AT EQUILIBRIUM IN THE ULTRACENTRIFUGE. I. THE PROTEIN CONCENTRATION DISTRIBUTION BY SCHLIEREN OPTICS AND THE NET HYDRATION IN CsCl SOLUTIONS<sup>1a</sup>

Ifft, James B.; Vinograd, Jerome

doi:10.1021/j100816a040

Cited by 48 publications

(17 citation statements)

References 6 publications

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“…Calculations of buoyant density, selective solvation and apparent molecular weight. These followed the procedures described by Hearst & Vinograd (1961b,c), Hearst, Ifft & Vinograd (1961) and Ifft & Vinograd (1962) and will accordingly be summarized only briefly.…”

Section: Methodsmentioning

confidence: 99%

“…The buoyant density of proteins in aqueous caesium chloride is approx. 1.3g/ml Ifft & Vinograd, 1962), whereas that of carbohydrates is approxiimately 1.6g/ml (Erikson & Szybalski, 1964). Accordingly, isopycnic equilibrium methods (see, e.g., Vinograd & Hearst, 1962) should be particularly useful for the preparation and characterization of blood-groupspecific glycoproteins, where a buoyant density intermediate between the extremes quoted may be expected.…”

mentioning

confidence: 99%

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The use of equilibrium-density-gradient methods for the preparation and characterization of blood-group-specific glycoproteins

Creeth

Denborough

1970

Biochemical Journal

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1. The method of sedimentation equilibrium in a gradient of caesium chloride has been applied to the preparation of blood-group-specific glycoproteins from human ovarian-cyst fluids: it is shown that virtually complete separation from contaminating protein is easily accomplished in a single step. 2. The glycoproteins isolated in this way have been characterized by analytical density-gradient experiments in both caesium chloride and caesium sulphate and values of the buoyant density, selective solvation and apparent molecular weight have been obtained. 3. In some cases, materials prepared from the same cysts by solvent extraction methods have also been characterized in these terms. 4. The selective solvation values are about 0.1 and 0.5g of water/g of glycoprotein in caesium chloride and caesium sulphate respectively. 5. The apparent molecular-weight values are much lower than the weight-average molecular weights, and it is shown that the origin of the discrepancy is heterogeneity in density of the glycoproteins. 6. Some sources of error in the interpretation of density-gradient schlieren patterns are examined.

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

The use of equilibrium-density-gradient methods for the preparation and characterization of blood-group-specific glycoproteins

Creeth

Denborough

1970

Biochemical Journal

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“…Density-gradient ultracentrifugation (Meselson et al 1957) was used to examine the possible association of polysaccharide and protein. Polysaccharides have buoyant densities in the range 1 ·6-2· 0 glml, depending on the nature of the supporting solvent (Dunstone 1969), and proteins usually have buoyant densities of less than 1· 4 g/ml (Cox and Schumaker 1961;Ifft and Vinograd 1962). Covalently associated proteins and polysaccharides would be expected to have buoyant densities in the range 1 ·4-2' 0 glml depending on the relative proportion of each.…”

Section: (D) Density-gradient Ultracentrifugationmentioning

confidence: 99%

A Water-soluble Arabinogalactan-Peptide From Wheat Endosperm

Fincher¹,

Stone²

1974

Aust. Jnl. Of Bio. Sci.

149

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The water-soluble polymeric components of wheat endosperm have been extracted by two different procedures and their chemical composition studied in detail. Water extracts of wheat flour that had first been treated with hot 80% ethanol contained only 2% protein, but if the ethanol treatment was omitted up to 20% of the extracted polymeric fraction was low-molecular-weight non-dialysable protein material. Density-gradient ultracentrifugation in caesium chloride solutions indicated that most of this protein was free, whereas the 2% protein in the water extract of ethanol-treated flottr was firmly bound to a polysaccharide. This bound protein (a peptide) was characterized by high levels of hydroxyproline (16-20% of the amino acids present).Fractional precipitation of the water-soluble components with ammonium sulphate enabled the separation of a high-molecular-weight arabinoxylan (xylose : arabinose = 1·6 -1 . 9) and a lowmolecular-weight arabinogalactan (galactose :. arabinose =approx. 1· 5), the latter. being associated with the hydroxyproline-rich peptide.

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“…(4) 02(dP/dr) w2r°o the only remaining quantities to be determined were POP the physical buoyant density, and (dP/dr)*, the density gradient at r°. A simple correction4 for the compressibil ty of the cesium chloride solution, at the pressure at r 0 in the rotating liquid column, was used to derive PO from PO.…”

Section: H -(3)mentioning

confidence: 99%

Physicochemical Properties of Purified Staphylococcal Enterotoxin B

Wagman¹,

Edwards²,

Schantz³

1964

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THE BUOYANT BEHAVIOR OF BOVINE SERUM MERCAPTALBUMIN IN SALT SOLUTIONS AT EQUILIBRIUM IN THE ULTRACENTRIFUGE. I. THE PROTEIN CONCENTRATION DISTRIBUTION BY SCHLIEREN OPTICS AND THE NET HYDRATION IN CsCl SOLUTIONS^1a

Cited by 48 publications

References 6 publications

The use of equilibrium-density-gradient methods for the preparation and characterization of blood-group-specific glycoproteins

The use of equilibrium-density-gradient methods for the preparation and characterization of blood-group-specific glycoproteins

A Water-soluble Arabinogalactan-Peptide From Wheat Endosperm

Physicochemical Properties of Purified Staphylococcal Enterotoxin B

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THE BUOYANT BEHAVIOR OF BOVINE SERUM MERCAPTALBUMIN IN SALT SOLUTIONS AT EQUILIBRIUM IN THE ULTRACENTRIFUGE. I. THE PROTEIN CONCENTRATION DISTRIBUTION BY SCHLIEREN OPTICS AND THE NET HYDRATION IN CsCl SOLUTIONS1a

Cited by 48 publications

References 6 publications

The use of equilibrium-density-gradient methods for the preparation and characterization of blood-group-specific glycoproteins

The use of equilibrium-density-gradient methods for the preparation and characterization of blood-group-specific glycoproteins

A Water-soluble Arabinogalactan-Peptide From Wheat Endosperm

Physicochemical Properties of Purified Staphylococcal Enterotoxin B

Contact Info

Product

Resources

About

THE BUOYANT BEHAVIOR OF BOVINE SERUM MERCAPTALBUMIN IN SALT SOLUTIONS AT EQUILIBRIUM IN THE ULTRACENTRIFUGE. I. THE PROTEIN CONCENTRATION DISTRIBUTION BY SCHLIEREN OPTICS AND THE NET HYDRATION IN CsCl SOLUTIONS^1a