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| Titel: |
Chemical and Enzymatic Derivatization of Carbohydrate Side Chains of Antifreeze Glycoproteins |
| Auteur: |
Feeney, Robert E. Osuga, David T. Yeh, Yin |
| Verschenen in: |
Journal of carbohydrate chemistry |
| Paginering: | Jaargang 13 (1994) nr. 3 pagina's 347-361 |
| Jaar: |
1994-04-01 |
| Inhoud: |
At this time there have been a variety of different fully or partially characterized proteins that have the function described as “antifreeze.”1-10 The proteins that have been studied for the longest time are antifreeze glycoproteins (AFGP). These are polymers of H2N[Ala-Ala(β-galactosyl(1→3)α-N-acetylgalactosamine)Thr]nAla-Ala-COOH (Figure 1), and they typically consist of a number of distinct components. Eight have been characterized (n = 50, 45, 35, 28, 17, 8, 5, and 4) AFGP 1 to AFGP 8, respectively. The small antifreeze polymers, AFGP 6-8, constitute over 80% of the total proteins and have some prolines following threonines.11 These are found in the antarctic fish families of Nototheniidae, Channichthyidae, and Bathydraconidae, as well as in the arctic fish, Boreogadus saida, Gadus morhua, Gadus ogac, and Microgadus tomcod. The arctic fish Eleginus gracilis also has very similar glycoproteins (EgAF) except that the major fractions, the smaller ones (EgAF 7R and EgAF 8R), have additional dipeptides at the C-terminal end consisting of arginine and alaninel12 (Figure 2). |
| Uitgever: |
Taylor & Francis |
| Bronbestand: |
Elektronische Wetenschappelijke Tijdschriften |
Details van artikel 40 van 252 gevonden artikelen
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