Determination of Diffusion Coefficients of Haemocyanin at Low Concentration by Intensity Fluctuation Spectroscopy of Scattered Laser Light

Foord, R.; Jakeman, E.; Oliver, C.J.; Pike, E. R.; Blagrove, R.J.; Wood, Edward J.; Peacocke, A. R.

doi:10.1038/227242a0

Cited by 207 publications

(57 citation statements)

References 13 publications

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“…Under these conditions it was found to have an sis of 25 S (compared with, for example, a value of 0.9 S for the siO,w for Fl [lo] ). The diffusion coefficient was, in fact, measurable at these concentrations (1.5 to 4 mg/ml) by intensity fluctuation spectroscopy [8] and was found to be 0.80 (kO.01) X lo-' cm' set-' . fig.…”

Section: Resultsmentioning

confidence: 99%

“…The diffusion coefficient at infinite dilution (D") of fraction F201 was determined by means of intensity fluctuation spectroscopy [8] and this yielded a molecular weight (MS/D) after combination with its sedimentation coefficient at infinite dilution by means of the Svedberg equation. Partial specific volumes of the histone fractions were determined at 25" by means of an Anton Paar Digital Densimeter.…”

Section: Methodsmentioning

confidence: 99%

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The molecular weights and association of the histones of chicken erythrocytes

Diggle¹,

Peacocke²

1971

FEBS Letters

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

The molecular weights and association of the histones of chicken erythrocytes

Diggle¹,

Peacocke²

1971

FEBS Letters

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“…The correlation function of the two separate components turned out to the monoexponential and the diffusion coefficients compared well with those obtained under non-flowing conditions as well as with those in the literature [7]. In samples of Fr-ATPase, a small amount of aggregated material was still present, and a two exponential analysis of the correlation function was applied by means of the non-linear fit program (Harwell Subroutine VCO 5A) modified by K. H. Mtiller and Th.…”

Section: Materandand and Methodsmentioning

confidence: 68%

Determination of diffusion coefficients and molecular weights of partially dissociated F₁‐ATPase from yeast by gel filtration coupled to laser light‐scattering spectroscopy

Doster¹,

Begusch²,

Hess³

1980

FEBS Letters

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“…Light-scattering by solutions has been used as a method for finding macromolecular parameters for the past 25 years. During the past decade, however, it has become possible, largely owing to the advent of the laser, to investigate the spectral distribution of the scattered light (see Cummins, Knable & Yeh, 1964;Dubin, Lunacek & Benedek, 1967;French, Angus & Walton, 1969;Rimai, Hickmott, Cole & Carew, 1970;Pecora, 1970;Ford, Karasz & Owen, 1970;Sellen, 1970;Foord et al 1970). The spectral linewidth, which is of the order of 1OOHz (about 10-9 ), arises from the thermal motion of the macromolecules.…”

Section: Iri8h Republic)mentioning

confidence: 99%

Light-scattering Raleigh linewidth measurements on G-actin

Graham

Sellen

1971

Biochemical Journal

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chloride). The rate and extent of superprecipitation of natural actomyosin fronm white fibres were 25-50% greater than those of natural actomyosin from red fibres. It remains to be established how the contraction times of the red fibres and the white fibres are related to their myosin adenosine triphosphatase activities.Briskey, E. J., Sayre, R. N. & Cassens, R. G. (1962). J.Fd Sci. 27, 6. Dubowitz, V. (1970) Muscle becomes hard and inextensible during the onset of rigor (Bendall, 1960), but during subsequent storage at 2°C there is a progressive increase in tenderness. The ability to maintain isometric tension is lost (Jungk, Snyder, Goll & McConnell, 1967), but the muscle does not regain its extensibility. These changes during storage are believed to be caused by post-mortem autolysis. A study of the myofibrillar ultrastructural changes over the storage period essential to an understanding of the nature of this autolysis is reported. Proteolysis in the sarcoplasmic fraction and release of lysosomal cathepsin D were also investigated.Bovine semitendinosus muscle was sampled immediately post mortem and after 24h, 4 days and 10 days storage at 20C for light and electron microscopy. The supernatants obtained after centrifuging homogenates from Oh, 2-day and 15-day post-mortem samples for 30min at lOOOg (ra,. 7.62 cm) at 40C were applied to an exponential sucrose density gradient in the BXIV aluminium zonal rotor and centrifuged for 45min at 43000g (ray. 4.7cm) at 50C. Collected fractions were analysed for protein (Schuel & Schuel, 1967) and cathepsin D activity ((Anson, 1937).The phase-contrast microscope showed a progressive increase in incidence of transverse fibre breaks during the storage period. These breaks always occurred in the I band.Pre-rigor myofibrils in the electron microscope had the appearance of resting muscle (Huxley, 1960). The Z lines showed a well-defined fibrillar pattern (Landon, 1970), which gradually turned amorphous during subsequent storage. The other components of the myofibril were not significantly affected by storage for 10 days. The ultrastructural locus of the fibre breaks seen in the light microscope was the Z line/I band junction (Revile, Joseph & Harrington, 1971).The amount of sedimentable protein decreased during storage. In pre-rigor samples 52.5% of the total protein was sedimentable, whereas 2-day samples showed 27.5% and 15-day samples only 18% sedimentable protein.The total activity of cathepsin D did not change appreciably over the storage period, but of this 84.5% was sedimentable in pre-rigor samples and 40.7 % after 15 days.The limited and specific ultrastructural disruption of the myofibrillar fraction occurring during storage would undoubtedly result in increased tenderness and loss of ability to mnaintain isometric tension. The sarcoplasmic fraction undergoes a more extensive autolysis, but all the cathepsin D activity does not seem to be released during storage. This agrees with Valin (1970). Anson, M. L. (1937). J. gen. Physiol. 20, 565. Bendall, J. R. (1960 Lig...

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Determination of Diffusion Coefficients of Haemocyanin at Low Concentration by Intensity Fluctuation Spectroscopy of Scattered Laser Light

Cited by 207 publications

References 13 publications

The molecular weights and association of the histones of chicken erythrocytes

The molecular weights and association of the histones of chicken erythrocytes

Determination of diffusion coefficients and molecular weights of partially dissociated F₁‐ATPase from yeast by gel filtration coupled to laser light‐scattering spectroscopy

Light-scattering Raleigh linewidth measurements on G-actin

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Determination of Diffusion Coefficients of Haemocyanin at Low Concentration by Intensity Fluctuation Spectroscopy of Scattered Laser Light

Cited by 207 publications

References 13 publications

The molecular weights and association of the histones of chicken erythrocytes

The molecular weights and association of the histones of chicken erythrocytes

Determination of diffusion coefficients and molecular weights of partially dissociated F1‐ATPase from yeast by gel filtration coupled to laser light‐scattering spectroscopy

Light-scattering Raleigh linewidth measurements on G-actin

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Determination of diffusion coefficients and molecular weights of partially dissociated F₁‐ATPase from yeast by gel filtration coupled to laser light‐scattering spectroscopy