It is known [21,22], that thermoaggregation of BSA in water
at moderate temperatures changes thermodynamic properties of
the protein decreasing significantly thermodynamic compatibility
of BSA with other proteins, for example, with ovalbumin. Since
the limited thermoaggregation of the globular protein can lead to
changes its conformation state, and electrical properties, as well as
activity of the protein in its saturated solutions, we assumed that
such thermomodification of BSA molecules can affect also on the
molecular and structural properties of the inter protein complexes.
BSA or plasma albumin is a well-known globular protein
(MW=67 kDa) that has the tendency to aggregate in macromolecular assemblies. Its three-dimensional structure is composed of three
domains, each one formed by six helices. Seventeen disulphide
bonds are located in BSA molecule. The most common molecular form is ellipsoid (4.1 nm ×14.1 nm) [23]. Gelatin is a protein
derived by partial hydrolysis of collagen. The protein is unique
in that it is made up of triplets of amino acids, gly-X-Y. The X
and Y can be any amino acid but the most common are proline
and 4-hydroxyproline, which have a five-member ring structure.
Helix-coil transition of gelatin and gelation of gelatin solutions
has been studied extensively in past [24]. Gelatin is well known,
widely used in industry for its textural and structuring properties
[25], and capacity to form interpolymer complexes with polyelectrolyte (see, for example, [5,26]). Gelatin–BSA mixtures are
well known and used in biomedical and controlled release areas
[27,28]
It is known [21,22], that thermoaggregation of BSA in waterat moderate temperatures changes thermodynamic properties ofthe protein decreasing significantly thermodynamic compatibilityof BSA with other proteins, for example, with ovalbumin. Sincethe limited thermoaggregation of the globular protein can lead tochanges its conformation state, and electrical properties, as well asactivity of the protein in its saturated solutions, we assumed thatsuch thermomodification of BSA molecules can affect also on themolecular and structural properties of the inter protein complexes.BSA or plasma albumin is a well-known globular protein(MW=67 kDa) that has the tendency to aggregate in macromolecular assemblies. Its three-dimensional structure is composed of threedomains, each one formed by six helices. Seventeen disulphidebonds are located in BSA molecule. The most common molecular form is ellipsoid (4.1 nm ×14.1 nm) [23]. Gelatin is a proteinderived by partial hydrolysis of collagen. The protein is uniquein that it is made up of triplets of amino acids, gly-X-Y. The Xand Y can be any amino acid but the most common are prolineand 4-hydroxyproline, which have a five-member ring structure.Helix-coil transition of gelatin and gelation of gelatin solutionshas been studied extensively in past [24]. Gelatin is well known,widely used in industry for its textural and structuring properties[25], and capacity to form interpolymer complexes with polyelectrolyte (see, for example, [5,26]). Gelatin–BSA mixtures arewell known and used in biomedical and controlled release areas[27,28]
การแปล กรุณารอสักครู่..
