Molecular weight determination and compositional analysis of dextran-protein conjugates using low-angle laser light scattering technique combined with high-performance gel chromatography.
The low-angle laser light scattering technique combined with high-performance gel chromatography was applied for characterization of the dextran-ovalbumin and dextran-lysozyme conjugates obtained from the mild heating in dry state, which is attracting interest as a way leading to stabilization of proteins and to production of proteins with excellent emulsifying or antimicrobial ability (Nakamura, S., Kato, A. and Kobayashi, K. (1991) J. Agric. Food Chem. 39, 647-650). According to the above technique, providing the information about the molecular weight distribution and the composition of the conjugates, one or two dextran molecules were found to be linked to one molecule of the proteins. In addition, each of the conjugates was shown to exist as an oligomeric assembly of which formation is promoted by an increase in the salt concentration of buffer. The observations suggest that the increase in the hydrophobicity of the protein moiety as a result of partial denaturation and the introduction of the hydrophilic dextran chain affords the conjugate an amphiphilic property.
Kato
A
A
Institute for Protein Research, Osaka University, Japan.
Kameyama
K
K
Takagi
T
T
D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003911:Dextrans / Q000737:chemistry*; D007834:Lasers; D008970:Molecular Weight; D009113:Muramidase / Q000737:chemistry*; D010047:Ovalbumin / Q000737:chemistry*; D012542:Scattering, Radiation
D003911:Dextrans; D010047:Ovalbumin; D009113:Muramidase