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Clinical Chemistry 47: 2012-2022, 2001;
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(Clinical Chemistry. 2001;47:2012-2022.)
© 2001 American Association for Clinical Chemistry, Inc.

Articles

Identification of {alpha}1-Antitrypsin Variants in Plasma with the Use of Proteomic Technology

Kevin Mills1, Philippa B. Mills1, Peter T. Clayton1, Andrew W. Johnson1, David B. Whitehouse2 and Bryan G. Winchester1a

1 Biochemistry Endocrinology and Metabolism Unit, Institute of Child Health at Great Ormond Street Hospital, University College London, 30 Guilford St., London WC1 N 1EH, United Kingdom.

2 Medical Research Council Human Biochemical Genetics Unit, Galton Laboratory, University College London, London NW1 2HE, United Kingdom.

aAuthor for correspondence. Fax 44-0207-404-6191; e-mail B.Winchester{at}ich.ucl.ac.uk.

Background: Proteomic technology permits the investigation of genetic metabolic diseases at the level of protein expression. Changes in the expression, polypeptide structure, and posttranslational modification of individual proteins can be detected in complex mixtures of proteins.

Methods: We used high-resolution two-dimensional polyacrylamide gel electrophoresis to separate isoforms of plasma proteins and detect abnormalities of mass and/or charge. We confirmed the identity of the separated proteins by in-gel digestion with proteases and N-glycanases and then analyzed the released peptides and glycans by matrix-assisted laser-desorption ionization–time-of-flight mass spectrometry.

Results: Complete characterization of the polypeptide sequences and glycosylation of {alpha}1-antitrypsin isoforms was achieved in plasma from controls and from patients with three different known {alpha}1-antitrypsin deficiencies and congenital disorder of glycosylation type Ia.

Conclusions: This study shows that proteomic techniques are a powerful and sensitive means of detecting changes in the amino acid sequence and abnormal posttranslational modifications of specific proteins in a complex biologic matrix.




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