A relationship between the molecular weights of macromolecules and their elution volumes based on a model for Sephadex gel filtration

Squire, Phil G.

doi:10.1016/0003-9861(64)90303-0

Cited by 195 publications

(27 citation statements)

References 13 publications

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“…1). An almost identical value was obtained when the mol wt was calculated using the equation proposed by Squire (26). PEP carboxylase from maize and other C4 plants (28) and spinach leaves (17) (3,20,28), sugarcane (7), and spinach (17).…”

Section: Resultssupporting

confidence: 56%

Purification and Properties of Phosphoenolpyruvate Carboxylase from Immature Pods of Chickpea (Cicer arietinum L.)

Singal

Singh²

1986

Plant Physiol.

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Phosphoenolpyruvate carboxylase (EC 4.1.1.31) was purified to homogeneity with about 29% recovery from immature pods of chickpea using ammonium sulfate fractionation, DEAE-cellulose chromatography, and gel filtration through Sephadex G-200 (9,22,23). In C4 plants, the enzyme levels in leaves are about 20-fold higher on a Chl basis than in C3 plants (9, 11) and the enzyme is localized in the cytoplasm of mesophyll cells (24). In addition to its role in C4 and CAM plants, relatively higher levels of PEP2 carboxylase have been reported in pod tissues of several legumes including chickpea (5, 10, 15). In these tissues, the enzyme has been suggested for reducing carbon losses by assimilating CO2 released during dark respiration or photorespiration; hence playing a major role in dark fixation of CO2. Though the enzyme has been well characterized from C4 and CAM plants (22)

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Section: Resultssupporting

confidence: 56%

Purification and Properties of Phosphoenolpyruvate Carboxylase from Immature Pods of Chickpea (Cicer arietinum L.)

Singal

Singh²

1986

Plant Physiol.

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“…Squire [41] and Ackers [20] have provided a theoretical basis for the physicochemical characterization of proteins by Sephadex gel filtration. The usefulness of correlating the behaviour of proteins on gel atration with their Stokes' radii is further demonstrated by the findings reported here.…”

Section: Discussionmentioning

confidence: 99%

Nitrite Reductase from Achromobacter fischeri: Molecular Weight and Subunit Structure

Husain

Sadana

1974

Eur J Biochem

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The Achromobacter fischeri nitrite reductase used in the present studies was monodisperse as judged by ultracentrifugation and disc-gel electrophoresis. The native enzyme has an average molecular weight of 80000 as determined by the Archibald approach-to-equilibrium method, disc-gel electrophoresis and from a combination of hydrodynamic properties. The sedimentation and diffusion coefficients are 5.25 S and 60.5 p.m2 s-l respectively, frictional ratio ( f / f o ) 1.25, and Stokes' radius 3.49 nm.Nitrite reductase does not dissociate in the presence of 6 M guanidine-HC1 or 6 M urea.The enzyme however splits into two physically indistingiushable subunits upon treatment with 6 M guanidine-HC1 in combination with lo/,, 2-mercaptoethanol or 101, sodium dodecylsulfate and 1 2-mercaptoethanol. In both the systems the subunit molecular weight has been found to be approximately 39000. Methionine is the sole N-terminal residue detected. These results indicate that Achromobacter nitrite reductase is composed of two subunits of equivalent size which are covalently bonded by a disulfi.de bridge.

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“…These models range from idealized pores (cones, cylinders and crevices [12] to a random pore structure with the assumption of norinally distributed pore radii [14].…”

Section: Discussionmentioning

confidence: 99%

Studies of the Distribution of Proteins Bound to CNBr‐Activated Sepharose 6B at the Electron‐Microscopic Level

Lasch

Iwig

Koelsch

et al. 1975

European Journal of Biochemistry

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Proteins were covalently attached to Sepharose by the CNBr method. Their distribution across the carrier beads was studied at the electron microscopic level. The approach has been to ferritinstain and to section the gel beads. Ferritin was either coupled directly to the polysaccharide backbone of the carrier or conjugated with pure rabbit anti-aminopeptidase in order to visualize covalently bound leucine aminopeptidase by the immunferritin technique. The results corroborate earlier fluorescence microscopic findings of a uniform protein distribution, provided that a nuinber of conditions are fulfilled.

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A relationship between the molecular weights of macromolecules and their elution volumes based on a model for Sephadex gel filtration

Cited by 195 publications

References 13 publications

Purification and Properties of Phosphoenolpyruvate Carboxylase from Immature Pods of Chickpea (Cicer arietinum L.)

Purification and Properties of Phosphoenolpyruvate Carboxylase from Immature Pods of Chickpea (Cicer arietinum L.)

Nitrite Reductase from Achromobacter fischeri: Molecular Weight and Subunit Structure

Studies of the Distribution of Proteins Bound to CNBr‐Activated Sepharose 6B at the Electron‐Microscopic Level

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