Computer analysis of sedimentation equilibrium data from paucidisperse and interacting systems

Reinhardt, William P.; Squire, Phil G.

doi:10.1016/0926-6585(65)90065-8

Cited by 14 publications

(3 citation statements)

References 6 publications

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“…A computer analysis of sedimentation equilibrium data for paucidisperse and interacting systems was reported (402).…”

Section: Centrifugationmentioning

confidence: 99%

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Biochemical Analysis

Hamilton¹

1966

Anal. Chem.

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review covers the two year period commencing January 1, 1964 through December 31,1965, following directly on the previous review of the same title (201) in Analytical Chemistry.Those papers which describe advances and improvements in methods and instrumentation as applied to determinations in the field of biochemistry are listed.Routine applications of standard methods are not reported. For these reasons, references to many excellent papers were omitted. Even with such an arbitrary selection, many papers of importance and interest had to be noted and as a consequence critical appraisal had to be virtually eliminated.COMMUNICATION AIDS, NEW JOURNALS, AND NEW BOOKS

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“…A computer analysis of sedimentation equilibrium data for paucidisperse and interacting systems was reported (402).…”

Section: Centrifugationmentioning

confidence: 99%

“…The sedimentation of chemically reacting, nondiffusing macromolecules was considered from a general theoretical standpoint (305) and for special cases solutions to the general equations were provided (306). A computer analysis of sedimentation equilibrium data for paucidisperse and interacting systems was reported (402).…”

Section: Centrifugationmentioning

confidence: 99%

Biochemical Analysis

Hamilton¹

1966

Anal. Chem.

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“…However, its use for chemically analysing interacting systems is inexact (Adams, 1969). Reinhardt & Squire (1965) were aware of the problem when they used this method to analyse results for interacting ovine interstitial-cell-stimulating hormone. They derived a term that corrected for the mutual dependence of the individual species when at equilibrium.…”

Section: Analysis Of Recordsmentioning

confidence: 99%

A comparison of the association of yeast phosphoglycerate mutase (EC2.7.5.3) with that of haemoglobin. An ultracentrifuge study

Spragg¹,

Roche²,

Wilcox³

1977

Biochemical Journal

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1. Previous work showed that yeast phosphoglycerate mutase (EC 2.7.5.3) has a mol.wt. of between 107000 and 110000. Preliminary examination showed that at dilutions less than 0.1 g/1 the enzyme dissociated into its subunits. 2. This dissociation was quantitatively examined by both equilibrium and velocity centrifugation. 3. The mathematical analysis of the equilibrium records was tested against oxyhaemoglobin in a variety of ionic strengths and at two temperatures. 4. The estimated L2,4 (interaction coefficient) for oxyhaemoglobin generally agreed with published values except at 6 degrees C in 0.9 M-NaCl, when it was 2.5 times larger than the published value. 5. Statistical analysis of ultracentrifugal-equilibrium experiments showed that the predominant reaction for phosphoglycerate mutase was monomer in equilibrium tetramer, to give an L1,4 of 40.3+/-23.4 (S.D.)1(3)-g(-3) at 20 degrees C. Decreasing the temperature decreased the association to given an enthalpy of between 40 and 60kJ/mol. 6. Analysis of velocity experiments carried out with concentrations varying from 0.3 to 17 g/1 gave an L1,4 of 3111(3)-g(-3). Incorporating errors from estimating S20,w into the analysis showed that this estimate could range from 893 to 1421(3)-g(-3). 7. The concentration-dependence of S20,w was 0.95 litre-g-1 and s020,w for the tetramer was 66.9ps. 8. These results are discussed in relation to the activity of the enzyme.

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Molecular weight distribution of interacting proteins calculated by multiple regression analysis from sedimentation equilibrium data: An interpretation of αs1-κ-casein interaction

Voort

Nakai

1979

Archives of Biochemistry and Biophysics

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Computer analysis of sedimentation equilibrium data from paucidisperse and interacting systems

Cited by 14 publications

References 6 publications

Biochemical Analysis

Biochemical Analysis

A comparison of the association of yeast phosphoglycerate mutase (EC2.7.5.3) with that of haemoglobin. An ultracentrifuge study

Molecular weight distribution of interacting proteins calculated by multiple regression analysis from sedimentation equilibrium data: An interpretation of αs1-κ-casein interaction

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