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Biopharmaceuticals glycosylation, therapeutic proteins

Many polypeptides undergo covalent modification after (or sometimes during) their ribosomal assembly. The most commonly observed such PTMs are listed in Table 2.7. Such modifications generally influence either the biological activity or the structural stability of the polypeptide. The majority of therapeutic proteins bear some form of PTM. Although glycosylation represents the most common such modification, additional PTMs important in a biopharmaceutical context include carboxylation, hydroxylation, sulfation and amidation these PTMs are now considered further. [Pg.29]

Technical advances facilitating genetic manipulation of animal cells now allow routine production of therapeutic proteins in such systems. The major advantage of these systems is their ability to carry out post-translational modification of the protein product. As a result, many biopharmaceuticals that are naturally glycosylated are now produced in animal cell lines. CHO and BHK cells have become particularly popular in this regard. [Pg.109]


See other pages where Biopharmaceuticals glycosylation, therapeutic proteins is mentioned: [Pg.238]    [Pg.58]    [Pg.226]    [Pg.129]    [Pg.390]    [Pg.53]    [Pg.155]    [Pg.45]    [Pg.663]    [Pg.2005]    [Pg.346]    [Pg.247]    [Pg.245]    [Pg.697]    [Pg.417]    [Pg.186]    [Pg.527]    [Pg.329]    [Pg.20]    [Pg.850]    [Pg.864]    [Pg.1031]    [Pg.351]    [Pg.267]    [Pg.632]    [Pg.507]    [Pg.237]    [Pg.233]   
See also in sourсe #XX -- [ Pg.99 , Pg.100 , Pg.101 , Pg.102 , Pg.103 , Pg.104 , Pg.105 , Pg.106 , Pg.107 , Pg.108 , Pg.109 , Pg.110 , Pg.111 , Pg.112 , Pg.113 , Pg.114 ]




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