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- W2020108680 abstract "The encephalitogenic basic protein from bovine spinal cord was treated with purified bovine brain proteinase (cathepsin D, EC 3.4.4.23) yielding 3–4 peptide fragments. An encephalitogenic fragment (peptide III-a, 8645 daltons) was purified by repetitive filtration on Sephadex gel. The purity of the peptide was established by polyacrylamide gel electrophoresis at acid and alkaline pH and by amino acid and end group analysis. The N- and C-terminal amino acid sequence of peptide III-a shows that the brain acid proteinase hydrolyzes the Phe-Phe linkage (residues 89–90) releasing the C-terminal 81 residues of the basic protein molecule." @default.
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- W2020108680 title "Hydrolysis of myelin basic protein with brain acid proteinase" @default.
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- W2020108680 doi "https://doi.org/10.1016/s0006-291x(74)80316-5" @default.
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