Proteases of HIV-1 and MAV Hydrolyze Specifically Human Apo-Hemopexin

Autor:	Iva Pichová, Zdeněk Voburka, Ivan Kluh, Věra Černá
Rok vydání:	2000
Předmět:	Proteases biology Chemistry Hemopexin General Chemistry Cleavage (embryo) Molecular biology Virus Deubiquitinating enzyme NS2-3 protease HIV-1 protease Biochemistry Cleave biology.protein
Zdroj:	Collection of Czechoslovak Chemical Communications. 65:1191-1197
ISSN:	1212-6950 0010-0765
DOI:	10.1135/cccc20001191
Popis:	The specificities of HIV-1 (Human Immunodeficiency Virus Type 1) and MAV (Myeloblastosis Associated Virus) proteases have been evaluated for their ability to split two-domain protein human apo-hemopexin. Both proteases hydrolyze only one peptidic bond Leu240-Ser241located in the connecting region between two domains. The ability of viral proteases to cleave Leu-Ser bond was confirmed by cleavage of synthetic octapeptide His-Leu-Val-Leu-Ser-Ala-Leu-Thr-NH2covering the susceptible area of human apo-hemopexin. The results demonstrate that the cleavage of Leu-Ser bond is not due to its location in the interdomain region of apo-hemopexin. The cleavable bond Leu-Ser has never been found either in viral or in non-viral proteins. According to the vector projection method this octapeptide was considered as non-hydrolyzable.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::a9a02ea99cfe117747b155b5881f2f7e https://doi.org/10.1135/cccc20001191 Zobrazit plný text záznamu