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Title: Studies on two abnormal human albumins : albumins Redhill and Warwick-2
Author: Brand, Sally
ISNI:       0000 0001 3477 0415
Awarding Body: University of Warwick
Current Institution: University of Warwick
Date of Award: 1983
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Albumins Redhill and Warwick-2 are monomeric, slow albumin variants discovered serendipitously in sera obtained from two unrelated families living in the U.K. Albumin Redhill was purified both by chromatofocusing and preparative polyacrylamide gel electrophoresis whereas albumin Warwick-2 was obtained exclusively by the latter technique. Following isolation, selective cleavage at methionine and tryptophan residues using specific chemical reagents was employed to examine the primary structure of each variant compared to the structure of normal albumin. Albumin Redhill is a proalbumin; the intracellular precursor of albumin. An amino acid substitution within the N-terminal propeptide has prevented normal cleavage of the additional residues in vivo. A second mutation lies in the C-terminal region of the sequence, probably between residues 503 and 585. This mutation is unusual in that it appears to involve the insertion of a short sequence, corresponding to approximately ten to twelve amino acids. The N-terminal residue is L-arginine; L-leucine was identified as the C-terminal end group. Albumin Warwick-2 contains an amino acid substitution in the N-terminal region of the sequence, between residues 1 and 87. This variant is not a proalbumin, having L-aspartic acid in the N-terminal position. The C-terminal residue is L-leucine. The isoelectric point of albumin Redhill is more acidic than that of albumin A, at pH 4.74-4.75, whereas albumin Warwick-2 becomes isoelectric on the basic side of albumin A, at pH 5.0-5.02. Both variants share a common antigenicity with albumin A and are present in a lesser quantity than the normal allotype in the serum. Albumin Redhill shows a reduced binding capacity for copper and nickel while albumin Warwick-2 binds these two metals normally. Both albumins show decreased binding for bilirubin and differential binding towards a series of organic dyes, but bind palmitate similarly to albumin A.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available
Keywords: QP Physiology