Autor:	Kiyoshi Miwa, Yoshiyuki Kumazawa, Katsunori Kobayashi, Shigeru Yamanaka
Rok vydání:	1996
Předmět:	chemistry.chemical_classification Tissue transglutaminase fungi Lysine Proteolytic enzymes Bacillus subtilis Biology biology.organism_classification Microbiology Bacillales Molecular biology Dithiothreitol Spore chemistry.chemical_compound Enzyme chemistry Biochemistry Genetics biology.protein Molecular Biology
Zdroj:	FEMS Microbiology Letters. 144:157-160
ISSN:	1574-6968 0378-1097
DOI:	10.1111/j.1574-6968.1996.tb08523.x
Popis:	Spores of Bacillus subtilis are resistant to proteolytic enzymes. Some of the spore coat proteins cannot be solubilized even by treatment with strong chemical agents like dithiothreitol. The spore coat has been suggested to possess cross-links between proteins in addition to disulfide bonds. We analyzed B. subtilis spore coat proteins to find specific cross-link structures. We detected ϵ-(γ-glutamyl)lysine in the spore coat proteins after sequential protease digestion followed by HPLC. We also detected transglutaminase activity in sporulating cells, which incorporated putrescine into N,N ′-dimethylcasein. This enzyme was suggested to create ϵ-(γ-glutamyl)lysine bonds between spore coat proteins.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::3925cc07f380c4916f8ff584492f976f https://doi.org/10.1111/j.1574-6968.1996.tb08523.x Zobrazit plný text záznamu Plný text