Studies on abnormal albumin
Albumin Mundey is a heat-stable monomeric, slow albumin variant. The mutation sites are located in CNBr fragments I (residues 1-87) and VI (residues 447-548). It does not have any additional peptide at the N- or C-terminal end as L-aspartic acid and L-leucine were detected as these respective residu...
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University of Warwick
1982
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| Online Access: | https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.345168 |
| Summary: | Albumin Mundey is a heat-stable monomeric, slow albumin variant. The mutation sites are located in CNBr fragments I (residues 1-87) and VI (residues 447-548). It does not have any additional peptide at the N- or C-terminal end as L-aspartic acid and L-leucine were detected as these respective residues. It is present in near equal quantity to normal albumin in serum and shares a common antigenicity with normal albumin. The isoelectric point of the defatted and native molecules are 5.7 and 5.0 respectively. The classification of its electrophoretic mobility using standard methods shows that it is similar to several Indian variants, but its dye binding properties are most similar to Albumin Kashmir. A study of its bilirubin binding capacity by the fluorescence-quenching method shows a slight impairment in binding. In a separate study, a rapid photo induced isomerisation of bilirubin-IXɑ was obtained in a buffer containing aqueous cationic detergent. Little isomerisation was detected under comparable conditions in anionic or neutral detergents. |
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