By Michael D. P. Boyle
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Methods 34, 93. Langone, J. J. (1982a). Adv. Immunol. 32, 157. Langone, J. J. (1982b). / . Immunol. Methods 55, 277. Langone, J. , Boyle, M. D. P, and Borsos, T. (1977). J. Immunol. 18,281. Methods Langone, J. , Boyle, M. D. P, and Borsos, T. (1978a). J. Immunol. 121, 327. Langone, J. , Boyle, M. D. P, and Borsos, T. (1978b). / . Immunol. 121, 333. 27 Chapter 2. Staphylococcal Protein A Lawman, M. J. , Boyle, M. D. , Gee, A. , and Young, M. (1984). J. Immunol. Methods 69, 197. , and Sjöquist, J.
Strains has also been reported by Colbert and Anilionis (1983), Guss et al. (1985), and Moks et al. (1986). The conclusion from these data is that protein A from S. aureus contains five IgG-binding regions. In Figure 3, the sequence of the IgG-binding regions are aligned to enable comparisons. , the closer the location of two regions, the higher the degree of homology. As already pointed out by Sjödahl (1977b), one interpretation of this phenomenon is that the primordial structural gene coding for the IgG-binding part of protein A has been subjected to stepwise gene duplications involving only one region followed by a period in which point mutations have occurred, thus generating slightly dissimi lar nucleotide and amino acid sequences.
1989). II. The Structure of the Gene A. The Signal Sequence Since protein A is an extracellular protein, the structural gene encodes an N-terminal signal peptide sequence, which is responsible for the translocation of the protein through the cell membrane (Figures 1 and 2). It was also found that this signal peptide sequence of 36 amino acids, which after cleavage leaves a mature protein with an MW of 53,697, was functional in several different species including E. , 1986a). This finding has also been confirmed by amino acid sequence analysis of isolated protein A from several of the aforementioned species by Abrahmsen et al.
Bacterial Immunoglobulin-binding Proteins by Michael D. P. Boyle