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, 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.
Taratina
T M
TM
All-Union Research Technology Institute of Antibiotics and Medical Enzymes, U.S.S.R. Academy of Sciences, Leningrad.
Potapenko VYe
Klenin
S I
SI
Bartoshevich
S P
SP
Volkova
L A
LA
Denisov
I G
IG
Moskvichev
B V
BV
D002942:Circular Dichroism; D007700:Kinetics; D008970:Molecular Weight; D011108:Polymers; D011487:Protein Conformation; D011760:Pyrrolidinones / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D013300:Streptokinase / Q000737:chemistry*; D014961:X-Ray Diffraction
D011108:Polymers; D011760:Pyrrolidinones; C042670:N-vinyl-2-pyrrolidinone; D013300:Streptokinase