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MYELIN BASIC-PROTEIN PURIFIED ON AN ION-EXCHANGE CONTINUOUS POLYMER BED IN THE PRESENCE OF ETHYLENE-GLYCOL AND SALT POSSESSES ACTIVITY AGAINST P-NITROPHENYL ACETATE
Uppsala University.
Uppsala University.
Uppsala University.
1995 (English)In: NEUROCHEMICAL RESEARCH, Vol. 20, no 6, 651-658 p.Other (Other scientific)
Abstract [en]

In this paper we describe a fast and mild method based on the use of a unique cation exchanger and buffers containing ethylene glycol and salt for the purification of the myelin basic protein (MBP; MW 18.5 kDa). MBP thus purified hydrolyses catalytically

Place, publisher, year, pages
PLENUM PUBL CORP , 1995. Vol. 20, no 6, 651-658 p.
Keyword [en]
MYELIN BASIC PROTEIN; ESTERASE ACTIVITY; ETHYLENE GLYCOL AND SALT; CONTINUOUS POLYMER BED; PERFORMANCE LIQUID-CHROMATOGRAPHY; SECONDARY STRUCTURE; MEMBRANE-PROTEINS; BRAIN MYELIN; IDENTIFICATION; SOLUBILIZATION; PURIFICATION; RENATURATION; CITRULLINE; S
Identifiers
URN: urn:nbn:se:uu:diva-68826OAI: oai:DiVA.org:uu-68826DiVA: diva2:96737
Note
Addresses: SEDZIK J, UNIV UPPSALA, DEPT BIOCHEM, BMC BOX 576, S-75123 UPPSALA, SWEDEN.Available from: 2008-10-17 Created: 2008-10-17

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