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Biomedical subjects

J Szopa

Publications and source records attributed to J Szopa.

46 records · Page 3Linked to original sources
PubMed1979

Effect of temporarily increased ionic strength and of urea on stability of DNA complexes with native and acetylated BPTI.

Hyperchromism of DNA-BPTI and DNA-acetylated BPTI complexes following dialysis/re-dialysis against solutions of increasing/decreasing concentrations of NaCl, urea or urea and NaCl, amounted to ca 50% of hyperchromism values obtained with free DNA or non-dialyzed complexes Stability of DNA-BPTI and DNA-acetylated BPTI complexes subjected to a temporary effect of NaCl, urea or urea and NaCl resembled stability of the complexes in the presence of Nacl or urea. The presence of all three geometrical DNA forms was detected in re-dialyzed DNA-BPTI and DNA-acetylated BPTI complexes. Possible mechanisms of interaction between BPTI and DNA are discussed.

Acetylation↗
PubMed1979

Interaction of DNA with guanidylated BPTI.

It was shown that guanidylated BPTI complexed with DNA stablized the native structure of the latter. It was found that hyperchromism values of DNA-guanidylated BPTI complexes, dialyzed against increasing and redialized against decreasing concentrations of NaCl or urea, amount ot ca 50% of hyperchromism values of free DNA or nondialyzed complexes. All three geometric forms of DNA were detected in DNA-guanidylated BPTI complexes subjected to the transient action of NaCl or urea.

Animals↗
PubMed1976

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.

Acetylation↗
PubMed1976

The effect of carboxymethylcellulose on antiproteolytic activity of unmodified, guanidylated and acetylated BPTI.

Acetylated BPTI loses its antitrypsin activity, but retains antichymotrypsin activity. Guanidylation diminishes the inhibitor's antitrypsin activity without affecting its antichymotrypsin activity. Acetylated inhibitor in complex with sodium salt of carboxymethylcellulose recovers antitrypsin activity which it did not have in the free state. Unmodified and guanidylated inhibitor in complex with CM-cellulose shows weaker antitrypsin as well as antichymotrypisn activity in comparison with free inhibitors.

Acetylation↗