[Formation and properties of S-protein complexes with S-peptide-containing hybrid polypeptides].
The fused polypeptides of human epidermal growth factor and one or two S-peptide of RNase A was shown to form stoichiometric (1:1) strong noncovalent and enzymatically active complexes with S-protein of RNase A. The dissociation constants for these complexes were found to be 5.0 x 10(-7) M and 1.1 x 10(-7) M. The complexes of polypeptides with S-protein were capable to hydrolyze ribopolynucleotides, and pyrimidine-2',3'-cyclophosphates specifically, like RNase S'. A possibility was shown of effective purification of the S-peptide-containing polypeptides by affinity chromatography in which S-protein is immobilized on solid supports.
Senchenko
V N
VN
Dianova
M V
MV
Kanevskiĭ
V Iu
VIu
Bocharov
A L
AL
Karpeĭskiĭ
M Ia
MIa
D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004815:Epidermal Growth Factor / Q000737:chemistry; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D012260:Ribonucleases / Q000737:chemistry*
D010446:Peptide Fragments; D010455:Peptides; D011993:Recombinant Fusion Proteins; C023560:ribonuclease S-peptide; D004815:Epidermal Growth Factor; D012260:Ribonucleases
Obrazovanie i svoĭstva kompleksov S-belka s S-peptidsoderzhashchimi gibridnymi polipeptidami.