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A B Mason

Showing results (71-80 of 78) with videos related to

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Biochemistry|February 24, 2000
Mutations at the histidine 249 ligand profoundly alter the spectral and iron-binding properties of human serum transferrin N-lobeQ Y He, A B Mason, R Pakdaman, et al.
Protein Expression and Purification|August 1, 1996
Production and isolation of the recombinant N-lobe of human serum transferrin from the methylotrophic yeast Pichia pastorisA B Mason, R C Woodworth, R W Oliver, et al.
Biochemistry|February 25, 1999
X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32M C Bewley, B M Tam, J Grewal, et al.
Biochemistry|May 25, 1993
Expression of glycosylated and nonglycosylated human transferrin in mammalian cells. Characterization of the recombinant proteins with comparison to three commercially available transferrinsA B Mason, M K Miller, W D Funk, et al.
The Biochemical Journal|October 15, 1996
Association of the two lobes of ovotransferrin is a prerequisite for receptor recognition. Studies with recombinant ovotransferrinsA B Mason, R C Woodworth, R W Oliver, et al.
The Biochemical Journal|August 15, 1997
Receptor recognition sites reside in both lobes of human serum transferrinA B Mason, B M Tam, R C Woodworth, et al.
The New England Journal of Medicine|March 9, 1972
Military medical educationL I Gardner, A J Bruwer, B R Krueger, et al.
Biochemistry|June 12, 1998
Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron releaseR T MacGillivray, S A Moore, J Chen, et al.
Pageof 8

Showing results (71-80 of 78) with videos related to

Sort By:
Pageof 8
You have reached the last page of results.This site can display upto 78 results.
Biochemistry|February 24, 2000
Mutations at the histidine 249 ligand profoundly alter the spectral and iron-binding properties of human serum transferrin N-lobeQ Y He, A B Mason, R Pakdaman, et al.
Protein Expression and Purification|August 1, 1996
Production and isolation of the recombinant N-lobe of human serum transferrin from the methylotrophic yeast Pichia pastorisA B Mason, R C Woodworth, R W Oliver, et al.
Biochemistry|February 25, 1999
X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32M C Bewley, B M Tam, J Grewal, et al.
Biochemistry|May 25, 1993
Expression of glycosylated and nonglycosylated human transferrin in mammalian cells. Characterization of the recombinant proteins with comparison to three commercially available transferrinsA B Mason, M K Miller, W D Funk, et al.
The Biochemical Journal|October 15, 1996
Association of the two lobes of ovotransferrin is a prerequisite for receptor recognition. Studies with recombinant ovotransferrinsA B Mason, R C Woodworth, R W Oliver, et al.
The Biochemical Journal|August 15, 1997
Receptor recognition sites reside in both lobes of human serum transferrinA B Mason, B M Tam, R C Woodworth, et al.
The New England Journal of Medicine|March 9, 1972
Military medical educationL I Gardner, A J Bruwer, B R Krueger, et al.
Biochemistry|June 12, 1998
Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron releaseR T MacGillivray, S A Moore, J Chen, et al.
Pageof 8