Zobrazeno 1 - 6 of 6 pro vyhledávání: '"Iu P, Bundulis"'
1
[Localization of an antigenic determinant of recombinant interleukin-2, recognized by monoclonal antibody 13B1]
Autor: V A, Skrivelis, Iu P, Bundulis, A V, Paniutich, N N, Voĭtenok, V E, Lunev, V A, Nesmeianov, A Iu, Tsimanis, E Ia, Gren
Publikováno v: Bioorganicheskaia khimiia. 17(6)
We suggest a simple approach to localization of antigenic determinants for the monoclonal antibody 13B1 raised against recombinant human interleukin-2. The approach is based on the limited trypsin proteolysis, peptide separation by the O'Farrell meth
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3a10dd9b81aad4b01dafa6bac1b467a8
https://pubmed.ncbi.nlm.nih.gov/1723267
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3
[Primary structure of the elongation factor G from Escherichia coli. VIII. Structure of tryptic peptides comprising the T4 fragment of limited trypsinolysis of the G-factor]
Autor: Iu B, Alakhov, M A, Bundule, Iu P, Bundulis, L M, Vinokurov, V P, Kozlov
Publikováno v: Bioorganicheskaia khimiia. 9(3)
Products of tryptic hydrolysis of the maleic anhydride modified fragment Th3 from limited thermolytic hydrolysis of the G-factor have been studied. Some short peptides which result from the trypsin action on the native G-factor molecule and belong to
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::92d9f345064f782540ea785440391b2d
https://pubmed.ncbi.nlm.nih.gov/6385999
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4
[Primary structure of the elongation factor G from Escherichia coli. VI. Structure of peptides of cyanogen bromide cleavage of the G-factor molecule]
Autor: Iu B, Alakhov, M A, Bundule, Iu P, Bundulis, L M, Vinokurov, V P, Kozlov
Publikováno v: Bioorganicheskaia khimiia. 9(3)
Peptides obtained as a result of cyanogen bromide cleavage of the G-factor have been studied. All 12 peptides embracing the whole structure of fragment T4 have been isolated. For their amino acid sequence determination, cyanogen bromide peptides have
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c3094afdd4168ab089005c397b575e05
https://pubmed.ncbi.nlm.nih.gov/6385997
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5
[Primary structure of the elongation factor G from Escherichia coli. VII. Study of peptides generated during hydrolysis of the T4 fragment by glutamic proteinase from Staphylococcus aureus]
Autor: Iu B, Alakhov, M A, Bundule, Iu P, Bundulis, L M, Vinokurov, V P, Kozlov
Publikováno v: Bioorganicheskaia khimiia. 9(3)
For fragment T4, obtained on limited trypsinolysis of the G-factor, the amino acid sequence embracing 76% of its structure has been determined by analysis of peptides resulting from the fragment T4 cleavage with staphylococcal glutamic protease. Thes
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e2d87de686f6849bd990f10d1383b4e6
https://pubmed.ncbi.nlm.nih.gov/6385998
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6
[Primary structure of the elongation factor G from Escherichia coli. IX. Structure of peptides generated by cyanogen bromide cleavage of the G-factor isolated on thiol-activated sepharose and of the products of the G-factor cleavage at Asp-Pro bonds. Complete primary structure]
Autor: Iu A, Ovchinnikov, Iu B, Alakhov, Iu P, Bundulis, M A, Bundule, L M, Vinokurov
Publikováno v: Bioorganicheskaia khimiia. 9(3)
The amino acid sequence of cysteine- and cystine-containing peptides resulting from cleavage of the G-factor by cyanogen bromide has been determined. For structure analysis cyanogen bromide peptides were further degradated using trypsin, chymotrypsin
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::224e88b3cae5de46e5366991aef22b1d
https://pubmed.ncbi.nlm.nih.gov/6386000
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