NDLI: Characterisation of recombinant unglycosylated human serum transferrin purified from Saccharomyces cerevisiae

Content Provider	Springer Nature Link
Author	Sargent, Peter J. Farnaud, Sebastien Cammack, Richard Zoller, Heinz M. P. Evans, Robert W.
Copyright Year	2006
Abstract	Structural identity between a recombinant transferrin mutant (N413Q, N611Q) secreted from Saccharomyces cerevisiae and the native protein was shown by CD analysis and immunodiffusion assays against anti-hSTf. The ability of the recombinant protein to bind iron was confirmed by urea–PAGE and EPR analysis of the iron-saturated protein revealed the characteristic holo-transferrin spectrum, indicating conservation of both iron-binding sites. The integrity of the unglycosylated recombinant protein indicates that such protein could be a valuable tool not only for structure–function characterisation but also crystallisation assays. In addition, the recombinant transferrin was found to be as effective as native transferrin as a growth factor in cell culture medium.
Starting Page	513
Ending Page	519
Page Count	7
File Format	PDF
ISSN	09660844
Journal	BioMetals
Volume Number	19
Issue Number	5
e-ISSN	15728773
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2006-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	characterisation iron recombinant Saccharomyces cerevisiae transferrin yeast Physical Chemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences

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Characterisation of recombinant unglycosylated human serum transferrin purified from Saccharomyces cerevisiae