Molecular characteristics of bovine serum albumin-dextran conjugates

Se Hyun Jung; Seung Jun Choi; Hyun Jung Kim; Tae Wha Moon

doi:10.1271/bbb.60026

Molecular characteristics of bovine serum albumin-dextran conjugates

Se Hyun Jung, Seung Jun Choi, Hyun Jung Kim, Tae Wha Moon

Dept. of Food Science and Technology

Research output: Contribution to journal › Article › peer-review

44 Scopus citations

Abstract

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 × 10⁵ g/mol and a less-abundant fraction with aggregates greater than 1:50 × 10⁶ g/mol. High-performance sizeexclusion 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.

Original language	English
Pages (from-to)	2064-2070
Number of pages	7
Journal	Bioscience, Biotechnology and Biochemistry
Volume	70
Issue number	9
DOIs	https://doi.org/10.1271/bbb.60026
State	Published - 2006

Keywords

Bovine serum albumin-dextran conjugate
Maillard reaction
Molar mass
Molar size
Multi-angle laser light scattering detector

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10.1271/bbb.60026

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abstract = "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 × 105 g/mol and a less-abundant fraction with aggregates greater than 1:50 × 106 g/mol. High-performance sizeexclusion 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.",

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AU - Jung, Se Hyun

AU - Choi, Seung Jun

AU - Kim, Hyun Jung

AU - Moon, Tae Wha

PY - 2006

Y1 - 2006

N2 - 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 × 105 g/mol and a less-abundant fraction with aggregates greater than 1:50 × 106 g/mol. High-performance sizeexclusion 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.

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KW - Molar size

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Molecular characteristics of bovine serum albumin-dextran conjugates

Abstract

Keywords

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