Myelin basic protein purified on an ion-exchange continuous polymer bed in the presence of ethylene glycol and salt possesses activity againstp-nitrophenyl acetate
- 1 June 1995
- journal article
- research article
- Published by Springer Nature in Neurochemical Research
- Vol. 20 (6) , 651-658
- https://doi.org/10.1007/bf01705531
Abstract
No abstract availableKeywords
This publication has 56 references indexed in Scilit:
- Limited Proteolysis of Myelin Basic Protein in a System Mimetic of the Myelin Interlamellar Aqueous SpaceJournal of Neurochemistry, 1993
- Identification of water-soluble proteases in myelin preparationsBiochemical and Biophysical Research Communications, 1992
- Esterase-Like Activity of Human Serum Albumin. VIII. Reaction with Amino Acid p-Nitrophenyl Esters.CHEMICAL & PHARMACEUTICAL BULLETIN, 1992
- Selective extraction, solubilization, and reversed‐phase high‐performance liquid chromatography separation of the main proteins from myelin using tetrahydrofuran/water mixturesJournal of Neuroscience Research, 1991
- Elucidation of cathepsin B‐like activity associated with extracts of human myelin basic proteinFEBS Letters, 1985
- On the binding of brain myelin basic protein to chromatographic resinsBiochemical and Biophysical Research Communications, 1985
- A new procedure for the isolation of the brain myelin basic protein in a lipid‐bound formFEBS Letters, 1984
- A study on the renaturation of membrane proteins after solubilization in SDS or following polyacrylamide gel electrophoresis in SDS, with special reference to a phosphatase from acholeplasma laidlawiiBiochimica et Biophysica Acta (BBA) - Biomembranes, 1983
- Microheterogeneity of bovine myelin basic protein studied by nuclear magnetic resonance spectroscopyBiopolymers, 1983
- The esterolytic activity of serum albuminBiochimica et Biophysica Acta, 1962