Poricin, an acidic protein with antitumor activity from a basidiomycete

Autor:	Roger T. Schillings, Hans W. Ruelius
Rok vydání:	1968
Předmět:	chemistry.chemical_classification Chromatography Magnesium Polyacrylamide Biophysics chemistry.chemical_element Biological activity Biochemistry Cellulose acetate Amino acid law.invention Electrophoresis chemistry.chemical_compound chemistry law Sephadex Crystallization Molecular Biology
Zdroj:	Archives of Biochemistry and Biophysics. 127:672-679
ISSN:	0003-9861
DOI:	10.1016/0003-9861(68)90277-4
Popis:	Poricin was crystallized from solutions of magnesium sulfate. Eighteen common amino acids were found in the hydrolyzates. Poricin is pigmented but contains no significant amounts of nonproteinaceous materials. The molecular weight was found to be about 100,000 by gel-filtration. Crystalline poricin appeared homogeneous by electrophoresis on polyacrylamide and chromatography on Sephadex but was shown to be inhomogeneous by electrophoresis on cellulose acetate and chromatography on DEAE-cellulose. The major component was obtained in electrophoretically pure form. It accounted for more than 80% of the total protein and was biologically active.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::c36ac82c8db7aa26be785198b6d501f7 https://doi.org/10.1016/0003-9861(68)90277-4 Zobrazit plný text záznamu