Interaction of basic polyvalent trypsin inhibitor before and after acetylation with DNA and carboxymethylcellulose.
1. The interaction of soluble complexes of DNA with basic polyvalent trypsin inhibitor of Kunitz's type before and after acetylation was studied. The ORD and CD spectra indicate that the secondary structure of DNA in complexes with protein undergoes marked alteration. 2. The Raman, ORD, CD and IR spectra showed that secondary structure of unmodified and acetylated polyvalent inhibitor in complexes with polyanoin undergoes marked alteration. Its content of alpha-spirals decreases, and content of beta-structure increases.
D000107:Acetylation; D000818:Animals; D002266:Carboxymethylcellulose Sodium; D002417:Cattle; D002942:Circular Dichroism; D004247:DNA; D008747:Methylcellulose / Q000031:analogs & derivatives; D008968:Molecular Conformation; D009690:Nucleic Acid Conformation; D009905:Optical Rotatory Dispersion; D013056:Spectrophotometry, Ultraviolet; D014361:Trypsin Inhibitors
D014361:Trypsin Inhibitors; D008747:Methylcellulose; D004247:DNA; D002266:Carboxymethylcellulose Sodium