Study of the structure of streptokinase conjugates with a hydrophilic vinylpyrrolidone copolymer

The modification of streptokinase by a synthetic N-vinylpyrrolidone copolymer leads to formation of conjugates varying in structures according to the proportions of the components in the reaction medium. Based on data obtained from spectrophotometry, as well as sedimentation and diffusion analyses,...

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Bibliographic Details
Published in:Biophysical chemistry 1990-10, Vol.38 (1), p.1-10
Main Authors: Taratina, T.M., Potapenko, V.Ye, Klenin, S.I., Bartoshevich, S.P., Volkova, L.A., Denisov, I.G., Moskvichev, B.V.
Format: Article
Language:English
Subjects:
Biological and medical sciences
Circular Dichroism
Conformational change
Conjugate structure
Fundamental and applied biological sciences. Psychology
Kinetics
Molecular biophysics
Molecular Weight
Polymers
Protein Conformation
Protein modification
Pyrrolidinones - chemistry
Reductive alkylation
Spectrophotometry, Ultraviolet
Streptokinase
Streptokinase - chemistry
Structure in molecular biology
Tridimensional structure
X-Ray Diffraction
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Summary:The modification of streptokinase by a synthetic N-vinylpyrrolidone copolymer leads to formation of conjugates varying in structures according to the proportions of the components in the reaction medium. Based on data obtained from spectrophotometry, as well as sedimentation and diffusion analyses, it is shown that in the presence of excess protein in the reaction medium, formation of the main chain takes place via the copolymer associated with several protein globules. Under conditions of excess modifier copolymer, either single-site and/or multiple-site bonding is possible for the protein backbone, depending on the molecular weight of the copolymer. One of the models for the conjugates obtained in this manner has been corroborated by small-angle X-ray scattering data. CD spectral analyses has been performed in order to demonstrate that covalent modification does not alter the secondary structure of streptokinase in the conjugate whereas the tertiary structure undergoes local changes in conformation.
ISSN:0301-4622
1873-4200
DOI:10.1016/0301-4622(90)80034-5