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Relation between Structure and Function in Some Partially Synthetic Ribonucleases S′.

Authors :
Filippi, Bruno
Moroder, Luis
Born, Gianfranco
Samartsev, Michele
Marchiori, Fernando
Source :
European Journal of Biochemistry. Mar75 Part 1, Vol. 52 Issue 1, p65-76. 12p.
Publication Year :
1975

Abstract

Some analogues have been prepared of S-peptide, the peptide obtained together with S-protein from subtilisin-modified beef pancreatic RNase A. The syntheses are described of [Orn10, Asn14]- S-peptide and 1∊,7δ-triguanidino-[Orn10, Asn14]-S-peptide. The S-peptide analogues are able to activate S-protein at the level of the parent [Orn10]-S-peptide and 1∊ ,7∊-diguanidino-S-peptide respectively, although at high peptide-to-protein molar ratios. After their recombination with S-protein the buried character of Tyr-25 was restored, as judged from difference absorption and circular dichroism spectra in the near-ultraviolet region. These findings indicate that the asparaginyl residue is a possible naturally occurring substituent in the RNase A sequences whose state of amidation in position 14 has not yet been defined. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00142956
Volume :
52
Issue :
1
Database :
Academic Search Index
Journal :
European Journal of Biochemistry
Publication Type :
Academic Journal
Accession number :
15801382
Full Text :
https://doi.org/10.1111/j.1432-1033.1975.tb03973.x