Structural studies of the apoprotein of the Folch-Pi bovine brain myelin proteolipid : characterization of the CNBr-fragments and of a long C-terminal sequence. |
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| Authors: | J Jollès F Schoentgen P Jollès M Vacher C Nicot A Alfsen |
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| Affiliation: | Laboratoire des Protéines, Université de Paris V, 45 rue des Saints-Pères, F-75270 Paris Cedex 06 France;Equipe de Recherche des Etats liés moléculaires, C.N.R.S., 45 rue des Saints-Pères, F-75270 Paris Cedex 06, France |
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| Abstract: | ![]()
The action of cyanogen bromide on the quite insoluble bovine proteolipid apoprotein allowed the determination of four peptide fragments: two of them constituted a 19 amino acid long C-terminal sequence of the apoprotein. Our results were in favour of the existence of only one subunit presenting a molecular weight closely related to 25,000 for which a schematic representation is given. |
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