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data on the myelin proteolipid of apparent molecular weight 20 kDa (DM-20)].\nBy a combination of chromatographic methods, we have obtained in an apparently homogeneous state the 24 kDa \"major myelin proteolipid\" (MMPL) and the 20 kDa \"myelin proteolipid\" (DM-20). Contrary to a commonly held view, the second one is not a conformationally different form of its major companion, as it differs markedly by its amino-acid composition, its electrophoretic behaviour after performic acid oxidation, and the results of tryptic digestion; however, they are obviously very closely related, as shown by the selective cleavages at the level of methionines and tryptophanes. These results are most simply interpreted by a single deletion in DM-20 of the hydrophilic fragment 100-140 of the (known) structure of the 24 kDa proteolipid. Lees' hypothesis of a deletion of fragment 197-267 cannot be retained."}

{"project":"oger-json-test","denotations":[{"id":"T6","span":{"begin":420,"end":430},"obj":"CHEBI:33709"},{"id":"T1","span":{"begin":80,"end":85},"obj":"P79826"},{"id":"T2","span":{"begin":225,"end":229},"obj":"PR:Q08351"},{"id":"T3","span":{"begin":268,"end":273},"obj":"P79826"},{"id":"T4","span":{"begin":285,"end":289},"obj":"A7MBU6"},{"id":"T5","span":{"begin":420,"end":425},"obj":"CHEBI:46882"},{"id":"T7","span":{"begin":420,"end":430},"obj":"CHEBI:33704"},{"id":"T8","span":{"begin":420,"end":430},"obj":"SO:0001237"},{"id":"T9","span":{"begin":426,"end":430},"obj":"CHEBI:37527"},{"id":"T10","span":{"begin":464,"end":473},"obj":"GO:0007610"},{"id":"T11","span":{"begin":480,"end":494},"obj":"C008817"},{"id":"T12","span":{"begin":490,"end":494},"obj":"CHEBI:37527"},{"id":"T13","span":{"begin":533,"end":542},"obj":"GO:0007586"},{"id":"T14","span":{"begin":723,"end":729},"obj":"SO:0000984"},{"id":"T15","span":{"begin":730,"end":738},"obj":"SO:0000159"},{"id":"T16","span":{"begin":742,"end":747},"obj":"P79826"},{"id":"T17","span":{"begin":767,"end":775},"obj":"SO:0000731"},{"id":"T18","span":{"begin":858,"end":866},"obj":"SO:0000159"},{"id":"T19","span":{"begin":870,"end":878},"obj":"SO:0000731"}],"text":"[Structural data on the myelin proteolipid of apparent molecular weight 20 kDa (DM-20)].\nBy a combination of chromatographic methods, we have obtained in an apparently homogeneous state the 24 kDa \"major myelin proteolipid\" (MMPL) and the 20 kDa \"myelin proteolipid\" (DM-20). Contrary to a commonly held view, the second one is not a conformationally different form of its major companion, as it differs markedly by its amino-acid composition, its electrophoretic behaviour after performic acid oxidation, and the results of tryptic digestion; however, they are obviously very closely related, as shown by the selective cleavages at the level of methionines and tryptophanes. These results are most simply interpreted by a single deletion in DM-20 of the hydrophilic fragment 100-140 of the (known) structure of the 24 kDa proteolipid. Lees' hypothesis of a deletion of fragment 197-267 cannot be retained."}