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Clin Chim Acta. 1988 Aug 31;176(2):179-84.

Characterisation of a slow component of normal human serum albumin.

Author information

1
Department of Clinical Biochemistry, Christchurch Hospital, New Zealand.

Abstract

A minor component of albumin was isolated from normal human serum. It had reduced electrophoretic mobility, reacted normally with specific albumin antiserum and, in contrast to normal albumin, did not bind nickel. Sequence analysis showed that the minor band contained components with Ala-His-Lys- and His-Lys- N-terminal sequences, indicating removal of Asp and Asp-Ala respectively from the parent albumin which was found to have the expected N-terminal sequence of Asp-Ala-His-Lys. Both normal albumin and the minor component had an average of 0.32 residues of glucose bound as fructosamine.

PMID:
3180465
DOI:
10.1016/0009-8981(88)90205-7
[Indexed for MEDLINE]

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