myelin-basic-protein and 4-nitrophenyl-acetate

myelin-basic-protein has been researched along with 4-nitrophenyl-acetate* in 1 studies

Other Studies

1 other study(ies) available for myelin-basic-protein and 4-nitrophenyl-acetate

Article	Year
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. Neurochemical research, 1995, Volume: 20, Issue:6 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 p-nitrophenyl acetate. This esterase activity facilitates not only the purification of MBP but also indicates that probably it is in its native state, i.e. there is a good chance that the purified molecules are structurally and chemically identical. This is a prerequisite to obtain crystals appropriate for x-ray diffraction and other studies. Topics: 4-Nitrophenylphosphatase; Amino Acid Sequence; Animals; Cattle; Chromatography, Ion Exchange; Detergents; Electrophoresis, Polyacrylamide Gel; Esterases; Ethylene Glycol; Ethylene Glycols; Female; Humans; Kinetics; Molecular Sequence Data; Molecular Weight; Myelin Basic Protein; Nitrophenols; Rabbits; Sequence Homology, Amino Acid; Sodium Chloride; Spinal Cord	1995

Article

Year

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.

Neurochemical research, 1995, Volume: 20, Issue:6

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 p-nitrophenyl acetate. This esterase activity facilitates not only the purification of MBP but also indicates that probably it is in its native state, i.e. there is a good chance that the purified molecules are structurally and chemically identical. This is a prerequisite to obtain crystals appropriate for x-ray diffraction and other studies.

Topics: 4-Nitrophenylphosphatase; Amino Acid Sequence; Animals; Cattle; Chromatography, Ion Exchange; Detergents; Electrophoresis, Polyacrylamide Gel; Esterases; Ethylene Glycol; Ethylene Glycols; Female; Humans; Kinetics; Molecular Sequence Data; Molecular Weight; Myelin Basic Protein; Nitrophenols; Rabbits; Sequence Homology, Amino Acid; Sodium Chloride; Spinal Cord

1995