Molecular characteristics of bovine serum albumin-dextran conjugates.
Bovine serum albumin (BSA)-dextran conjugates were prepared by using the Maillard reaction; depending on the ratio of dextran to BSA used, about 0.5-1 mol of dextran could be bound to 1 mol of native BSA. SDS-PAGE patterns revealed that BSA and dextran had been covalently bonded. Structural analyses by fluorescence spectroscopy and circular dichroism indicated that the BSA surface in each conjugate was covered with dextran without any great disruption of the native conformation. The conjugates could be grouped into two fractions on the basis of the weight-average molecular mass measured: the main fraction at 1.95-2.35 x 10(5) g/mol and a less-abundant fraction with aggregates greater than 1.50 x 10(6) g/mol. High-performance size-exclusion chromatography in conjunction with multi-angle laser light scattering detection revealed that the BSA-dextran conjugates prepared by using the Maillard reaction had various molar masses and radii.
Jung
Se Hyun
SH
Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Seoul National University, Seoul, Korea.
Choi
Seung Jun
SJ
Kim
Hyun Jung
HJ
Moon
Tae Wha
TW
D002850:Chromatography, Gel; D002942:Circular Dichroism; D003911:Dextrans / Q000138:chemical synthesis / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D015416:Maillard Reaction; D008970:Molecular Weight; D012542:Scattering, Radiation; D012710:Serum Albumin, Bovine / Q000138:chemical synthesis / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
D003911:Dextrans; C043578:bovine serum albumin-dextran conjugate; D012710:Serum Albumin, Bovine