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Cysteine relative hydrophobicity

Examination of the bovine and chicken sequences (Fig. 4) indicates that the amino terminal end of the chain is fairly polar whereas the carboxy terminal portion is relatively hydrophobic. There are no unusual features in composition or sequence of either of the vertebrate enzymes except that the amino terminal residue of chicken GDH is consistently found as cysteic acid (133 58) the first time this residue has been encountered in a protein. It is unknown whether or not it exists in this form in vivo, but isolation of the enzyme under reducing conditions still gave NHa-terminal cysteic acid, whereas six other residues were always found as cysteine. [Pg.336]

See other pages where Cysteine relative hydrophobicity is mentioned: [Pg.10]    [Pg.377]    [Pg.31]    [Pg.30]    [Pg.30]    [Pg.11]    [Pg.207]    [Pg.137]    [Pg.58]    [Pg.195]    [Pg.7]    [Pg.153]    [Pg.70]    [Pg.160]    [Pg.653]    [Pg.148]    [Pg.68]    [Pg.285]    [Pg.269]    [Pg.88]    [Pg.247]    [Pg.344]    [Pg.225]    [Pg.237]    [Pg.190]    [Pg.193]    [Pg.303]    [Pg.52]    [Pg.537]    [Pg.124]    [Pg.38]    [Pg.143]    [Pg.210]    [Pg.199]    [Pg.123]    [Pg.691]    [Pg.409]    [Pg.95]    [Pg.58]    [Pg.309]    [Pg.223]    [Pg.96]    [Pg.227]    [Pg.301]    [Pg.120]    [Pg.2053]    [Pg.153]    [Pg.47]    [Pg.762]    [Pg.296]   
See also in sourсe #XX -- [ Pg.342 ]



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Relative hydrophobicity

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