Amino terminal sequence of type 3 streptococcal M protein extraction products
| Autor: | Ivan Kluh, Jiří Havlíček, L. Morávek, Otto Kühnemund, Manfred Pavlík |
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| Rok vydání: | 1990 |
| Předmět: | |
| Zdroj: | Collection of Czechoslovak Chemical Communications. 55:2562-2567 |
| ISSN: | 1212-6950 0010-0765 |
| DOI: | 10.1135/cccc19902562 |
| Popis: | The amino terminal hypervariable part of the M protein molecule was chosen as a basis for the preparation of a synthetic peptide vaccine against group A streptococci. As part of the mapping of various serological types the main products of extraction of type M Streptococcus pyogeneswith limited pepsin (Pep) hydrolysis at pH 5.5 and with phage-associated lysin (PAL) were sequenced. Two entirely different sequences were obtained. The sequence of PAL M3 shows the absence of the α-helical potential in the shorter N-terminal region as is characteristic of the N-terminus of the M protein molecule. The main product of limited hydrolysis Pep M3 (pH 5.5), which shows the presence of the α-helical potential from the very amino terminal residue of its chain, does not involve most likely the proper N-terminus of the M protein. Extraction with pepsin under conditions of very limited proteolysis (pH 5.8) yielded a fragment with N-terminal sequence identical with that of PAL M3 (extracted nonproteolytically). |
| Databáze: | OpenAIRE |
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