Degree of linear polarization method for determination of intrinsic optical anisotropy of southern bean mosaic virus

Sano, Yoh

doi:10.1002/bip.360330108

Cited by 6 publications

(5 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Determination of Molecular Weight. The apparent weight-average molecular weight was measured by the intensity of light scattered at 90°angle and at a wavelength of 436 nm with the instrument of a modified ellipsometer, an automatic light scattering analyzer AEP-100 (Shimadzu Co., Ltd., Kyoto, Japan) (Sano, 1988(Sano, , 1990(Sano, , 1993Ishigami et al, 1995). The temperature was kept constant by circulating thermostatically controlled water.…”

Section: Methodsmentioning

confidence: 99%

Self-Assembling of Peptide α-1 of Globin Hydrolysates

Liu¹,

Yonekura²,

Tsutsumi³

et al. 1997

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

Globin is an edible protein in a large quantity from animal blood. However, globin shows a rather low solubility at neutral pH and little advantage in comparision with other proteins applied to the food industry. To improve its functional properties and to make clear the mechanism of gel formation, the hydrolysis of globin was performed with 0.8 M citric acid. The peptide α-1 was obtained by cleavage of the peptide bond between Asp-94 and Pro-95 in the α-chain of globin with 0.8 M citric acid. Physicochemical properties and structural characterization of peptide α-1 of globin hydrolysates were studied by amino acid sequence analysis, hydrophobic interaction chromatography, and circular dichroism (CD) spectra. The peptide α-1 was very highly hydrophilic on hydrophobic chromatography. The concentration dependence of peptide α-1 indicated the dissociation and association behaviors analyzed by a light scattering method. Circular dichroism spectra showed that the content of the α-helix and β-sheet structures of peptide α-1 were very different from the intact α-chain. We have also found that peptide α-1 played a role in transformation of aggregates of globin hydrolysates to gel. These results suggest that peptide α-1 acts as a cross-linker between the aggregate of globin hydrolysates through the transformation process of gel. Keywords: Globin; globin hydrolysates; peptide α-1; CD spectra

show abstract

Section: Methodsmentioning

confidence: 99%

Self-Assembling of Peptide α-1 of Globin Hydrolysates

Liu¹,

Yonekura²,

Tsutsumi³

et al. 1997

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

show abstract

“…Light Scattering Measurements. Measurements of the intensity of the light scattering were done with a modified Ellipsometer, an automatic light scattering analyzer AEP-100 (Shimadzu Co., Ltd.), at 20 °C (Sano, 1988(Sano, , 1990(Sano, , 1993. The linearly polarized monochromatic incident light passed through the cylindrical scattering cell, and the light scattered at scattering angle θ was detected through the linear analyzer by a photomultiplier in a telescope arm that can rotate from 45°to 135°by a stepping motor.…”

Section: Methodsmentioning

confidence: 99%

“…Light Scattering. Tertiary structure of the aggregates in solution was measured with a light scattering method (Sano et al, 1988(Sano et al, , 1990(Sano et al, , 1993. Figure 6 shows the light scattering pattern of the aggregates, in which KC/R θ is plotted against sin 2 (θ/2).…”

Section: Aggregate Formation Of Hydrolyzed Globinmentioning

confidence: 99%

Physicochemical Properties of Aggregates of Globin Hydrolysates

Liu

Yonekura

Tsutsumi

et al. 1996

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

Globin is an edible protein that is obtained in large quantity from animal blood. It can be used as an ingredient in a variety of meat products. However, globin showed a rather low solubility at neutral pH and little advantage compared with other proteins used in the food industry. The effective use of latent materials is an important research area in food science. This study succeeds in improving globin's functional properties and explaining the mechanism of gel formation. The hydrolysis of globin was performed with 0.8 M citric acid. The globin hydrolysates showed eight bands by tricine−SDS−PAGE having molecular masses that ranged from 5000 to 15 000 Da. The results of gel filtration chromatography indicated that the large aggregates were formed easily in the case of the globin hydrolysates. Physicochemical properties of aggregates of globin hydrolysates were studied by light scattering measurement and transmission electron microscope. It is clear that the aggregates were composed of two kinds of polypeptides, one of which, the β-chain, originated from the native globin and another, β-1, originated from the β-chain by cleavage between 99 (Asp) and 100 (Pro) of the β-chain through noncovalent bonding. By comparison with the position of standard protein (thyroglobulin, MW 669 000 Da), the molecular mass of the aggregate was estimated as above 700 000 Da. The aggregates of globin hydrolysate in solution approximated the thin rod-shaped model and had lengths of 130−140 nm by light scattering measurement. Electron micrography also showed the aggregates to consist of the thin rod aggregates. The molecular mass of the aggregates was determined to be 870 000 Da by light scattering measurement, indicating that the aggregate consists of 33−34 units because each unit was in the ratio of 1:1 complex of β-chain and β-1 with molecular masses of 16 000 and 10 900 Da, respectively. Keywords: Globin; globin hydrolysates; aggregates; light scattering; tricine−SDS−PAGE

show abstract

“…In general, the RNA chain in an aqueous solution tends to aggregate due to its high molecular weight, and therefore, filtration with a filter of pore size 0.45 μm (Millipore filter) was carried out , right before CD or SAXS measurements so that the solution thus filtered would involve monomer RNA only. Then, all sample solutions were further dialyzed against 0.1 mol L -1 phosphate buffer (ionic strength S = 0.2) at 4 °C.…”

Section: Methodsmentioning

confidence: 99%

Studies on the Conformation of a Polyelectrolyte in Solution: Local Conformation of Cucumber Green Mottle Mosaic Virus RNA Compared with Tobacco Mosaic Virus RNA

et al. 2007

Self Cite

View full text Add to dashboard Cite

The thermal stability of the local structures of cucumber green mottle mosaic virus RNA, CGMMV-RNA, and tobacco mosaic virus RNA, TMV-RNA, was studied by circular dichroism (CD) and small-angle X-ray scattering (SAXS) and compared with each other in the temperature domain from 20 to 50 degrees C. The temperature dependence of the molar ellipticity and mean-square radius of the cross section of a chain shows that the structure of CGMMV-RNA is more vulnerable than that of TMV-RNA. Such a different thermal stability of their structures was also reflected in the temperature dependence of the length and number of the constituent rods when the structures of the two RNA chains were represented by a model which consisted of rods joined with freely hinged joints. From these results, a possibility was suggested that the structural stability of CGMMV-RNA and TMV-RNA might be correlated with the infectivity of the corresponding virus, CGMMV and TMV, respectively.

show abstract

Degree of linear polarization method for determination of intrinsic optical anisotropy of southern bean mosaic virus

Cited by 6 publications

References 23 publications

Self-Assembling of Peptide α-1 of Globin Hydrolysates

Self-Assembling of Peptide α-1 of Globin Hydrolysates

Physicochemical Properties of Aggregates of Globin Hydrolysates

Studies on the Conformation of a Polyelectrolyte in Solution: Local Conformation of Cucumber Green Mottle Mosaic Virus RNA Compared with Tobacco Mosaic Virus RNA

Contact Info

Product

Resources

About