Dicyclohexylcarbodiimide-binding sites in the myelin proteolipid
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cellular and Molecular Neuroscience,General Medicine,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/BF00964677.pdf
Reference13 articles.
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3. Sebald, W., Machleidt, W., andWachter, E. 1980. N,N?-Dicyclohexylcarbodiimide binds specifically to a single glutamyl residue of the proteolipid subunit of the mitochondrial ATPases from Neurospora crassa and Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 77:785?789.
4. Hoppe, J., Schairer, H. U., andSebald, W. 1980. Identification of amino acid substituents in the proteolipid subunit of the ATP synthase from dicyclohexylcarbodiimide-resistant mutants of Escherichia coli. Eur. J. Biochem. 112:17?24.
5. Yoshida, M., Poser, J. W., Allison, W. S., andEsch, F. S. 1981. Identification of an essential glutamic acid residue in the beta subunit of the ATPase from the thermophilic bacterium PS3. J. Biol. Chem. 256:148?153.
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