Biomedical Engineering Reference
In-Depth Information
Chapter 9
S
TRUCTURAL
I
NVESTIGATION OF THE
I
NTERACTION
BETWEEN
B
OVINE
S
ERUM
A
LBUMIN AND
A
CID
G
ELATIN IN
W
ATER
Y. A. Antonov,
*
I. L. Zhuravleva and I. G. Plaschina
N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences,
Moscow, Russia
A
BSTRACT
This work studies interactions between a small globular protein and a relatively large
protein with a conformationally variable chain using dynamic light scattering,
differential scanning calorimetry, circular dichroism, fluorescence, and absorption
measurements. It uses the dilute and semidilute system water/bovine serum albumin
(BSA)/acid gelatin as a model. Gelatin molecules are able to form interpolymeric
complexes with BSA in water at the temperatures above the temperature of the
conformation transition and BSA/gelatin ratio ~6:1 (mole/mole). Interpolymer interaction
leads to collapse gelatin macromolecules due to their lost of the total negative charge,
partial stabilization of the secondary structure (increase the mean helix content), and
stabilization of BSA molecules against thermo aggregation. At the same time, the thermo
aggregation process of BSA molecules passes ahead of their thermodenaturation process.
Keyword:
Bovine serum albumin, acid gelatin, interaction, structure formation, protein
aggregation, conformation changes
I
NTRODUCTION
Investigations on the mechanism of complexation and the molecular characteristic of
protein-protein complexes play an important role in biotechnology and various fields of pure
and applied science[1]. When two or more proteins
bind together, often to carry out their
Search WWH ::
Custom Search