Download Albumin: Structure, Function and Uses by V.M. Rosenoer PDF

By V.M. Rosenoer

ISBN-10: 0080196039

ISBN-13: 9780080196039

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Extra resources for Albumin: Structure, Function and Uses

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Similar analyses of domains "two" versus "three" and "one" versus "three" show 20% and 18% identity, respectively. The somewhat greater similarity between domains "one" and "two" indicates that tandem duplication of a single domain gene first gave rise to domains "two" and "three", and after passage of some time to allow divergence in sequence of these domains, a tandem half gene duplication added "domain one", thus giving the triple {Continuation of Caption to Fig. 10 on facing page) that this structure was introduced by convergent evolution after separation from the globin gene, (c) The basic subdomain structure was doubled to give a two-subdomain structure shown here as subdomain " B " and " C " .

We are still missing sequence and overlap evidence for positions 400-403. In HSA these positions are occupied by Lys/Phe-Gln-Asn-, but in HSA we are also missing an overlap linking Lys and Phe. In our previous sequence <25) an error at 468-469, Glu-Ser, has been corrected in Fig. 1 to read Ser-Glu. Overall I believe that the BSA sequence in Fig. 1 is essentially correct. The overlapping problems at 195 and 400-403 allow the possibility of a few missing residues, but do not allow the mislocation of any large pieces of sequence.

16) Our evidence is weak as it is based only on a chymotryptic peptide Ala-Thr-Lys-Tyr which was isolated in very low yield. We therefore prefer McMenamy's sequence which appears to be satisfactory. We also prefer McMenamy's evidence for Lys-199 to our weak evidence for Arg at that position. Differences at 177 and 186-192 (16) now agree with our findings in the revised sequence of McMenamy in this book (p. 153). We find both Glu and Gin at 221 and propose that Glu is more likely the result of deamidation rather than a variant sequence.

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