Chicken amino acid sequences

Shinina M.E., Carlini P, Polticelli F., Zappacosta F., Bossa F., and Calabrese L. (1996), Amino acid sequence of chicken Cu, Zn-containing superoxide dismutase and identification of glutathionyl adducts at exposed cysteine residues, Eur. J. Biochem. 237(2), 433-439. 

Fig. 4. Amino acid sequence of several histone HI proteins to illustrate the macroheterogeneity of linker histones. Amino acid sequence of two highly specialized development-specific members of the histone HI family. A. Oocyte specific mammalian histone Hlfo (previously Hloo) [116]. B. PL-I (EM-1/6) protein from the sperm of the razor clam Ensis minor [120]. These two sequences are shown in comparison to the highly specialized histone H5 from chicken erythrocytes. The regions corresponding to the trypsin-resistant (winged helix motif [96]) which is characteristic of the protein members of the histone HI family are indicated by a box and have been aligned to show the sequence similarity.

While invertebrate tropomyosins are likely pan-allergens, vertebrate tropomyosins appear to be nonallergenic (Reese et ah, 1999). Using bioinformatics approaches to compare the sequences of tropomyosins from various species, Goodman et ah (2002) determined that tropomyosins from vertebrate species — rabbit, pig, chicken, and human — share 53-57% amino acid sequence identity to the known shrimp tropomyosin allergen. Met e 1. This comparison likely explains why vertebrate tropomyosins are not allergenic and do not cross-react with IgE antibodies specific to invertebrate tropomyosins. 

Fig. 1. Amino acid sequence of chicken Cx43 according to Veenstra et al. [1993]. Possible targets for phosphorylating enzymes are underlined.

Figure 4.5. PIR format for amino acid sequence of chicken egg-white lysozyme.

Figure 12.9. Protein structure prediction with PHD. The amino acid sequence of chicken lysozyme precursor (147 amino acids) is submitted to PredictProtein server for PHD structure predictions. The returned e-mail reports protein class based on secondary structures, predicted secondary structure composition (%H, %E, and %L), residue composition, data interpretation, and predicted data in two levels (brief and normal of which the normal is shown). Search for the database can be performed by making choice(s) from the list(s) of pop-up box(es).

Fig. 2. Alignment of the amino acid sequence of H. volcanii DHFR with the amino acid sequences of DHFRs of E. coli, L. casei, and chicken liver. From Zusman et al. (1989), with permission.

Kato, I., Schrode, J., Kohr, W.J., Lakowski, M. Jr. 1987. Chicken ovomucoid Determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all three of its domains. Biochemistry 26 193-201. 

T10. Turk, V., Brzin, J., Longer, M., Ritonja, A., Eropkin, M., et al., Protein inhibitors of cysteine proteinases. III. Amino-acid sequence of cystatin from chicken egg white. Hoppe Seylers Z. Physiol. Chem. 364(11), 1487-1496(1983). 

G. (1975). Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 A resolution using amino acid sequence data. Nature 255, 609-614. 

The large size of transferrins (670-700 residues), with the consequent difficulties of chemical sequencing, meant that it was not until 1982 that the first amino acid sequences, those of human serum transferrin 10) and chicken ovotransferrin 34,35), were established. These were closely followed by that of human lactoferrin 11). The twofold internal repeat in each sequence (see below) was immediately apparent, and comparison of all three sequences then identified conserved tyrosines and histidines that were potential ligands for iron (11). 

Since that time many more sequences have become available through the advent of recombinant DNA technology and the deduction of amino acid sequences from the base sequences of cloned DNA. At the present time, the primary structures (amino acid sequences) of 14 proteins of the transferrin family have been established. These include seven serum transferrins, from human 10, 36), pig (37), horse 38), rabbit 39), toad Xenopus laevis) 40), sphinx moth (M. sexta) 13), and cockroach Blaberus discoidalis 4) chicken 34, 35) and duck 41) ovotransfer-rins four lactoferrins, from human (11, 42), mouse 43), pig 44) and cattle 45, 46) and the human tumor cell melanotransferrin 47). All of these sequences are available from sequence databases such as EMBL and SWISSPROT. 

Geisler N, Weber K. The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins. EMBO J. 1982 1 1649-1656. 

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