Clinical Chemistry
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Clinical Chemistry 50: 257-259, 2004; 10.1373/clinchem.2003.026625
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(Clinical Chemistry. 2004;50:257-259.)
© 2004 American Association for Clinical Chemistry, Inc.


Letters

Cross-Reactivity of Three Recombinant Insulin Analogs with Five Commercial Insulin Immunoassays

William E. Owen1 and William L. Roberts2,a

1 ARUP Institute for Clinical and Experimental Pathology Salt Lake City, UT
2 Department of Pathology University of Utah Health Sciences Center Salt Lake City, UT

aAddress correspondence to this author at: c/o ARUP Laboratories, 500 Chipeta Way, Salt Lake City, UT 84108. Fax 801-584-5207; e-mail william.roberts@aruplab.com.

The first 20% of the full text of this article appears below.


To the Editor:

Several new insulin analogs that are prepared with recombinant DNA technology are available for clinical use [for a recent review, see Ref. (1)]. These agents have altered pharmacokinetics compared with regular human insulin. Insulin aspart (NovoLogTM; Novo Nordisk Pharmaceuticals) is homologous with regular human insulin except for a single substitution of aspartic acid for proline at position B28. This single substitution reduces the molecule’s tendency to form hexamers. Therefore, insulin aspart is absorbed more rapidly after subcutaneous injection and has both a faster onset of action and a shorter duration of action than regular insulin. A second short-acting recombinant insulin is insulin lispro (Humalog®; Eli Lilly and Company), which is a human insulin analog created by reversing the amino acids at positions 28 (Pro to Lys) and 29 (Lys to Pro) of the B chain. It is absorbed more rapidly than regular human insulin when administered subcutaneously and has a shorter duration of action.

A third recombinant insulin that is longer acting is insulin glargine (Lantus®; Aventis Pharmaceuticals), which differs from regular human insulin by the substitution of glycine for asparagine at position A21 and by the addition of two arginine residues to the COOH terminus of the B chain. These modifications lead to a slower, more prolonged absorption than regular insulin and a relatively stable concentration–time profile over 24 h. Insulin glargine is partially metabolized at the COOH terminus of the B chain in the subcutaneous depot to form two active metabolites, M1 and M2, with in vitro activity . . . [Full Text of this Article]




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Plasma insulin concentrations during a hyperinsulinaemic clamp: what do we measure?
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S. E. Manley, I. M. Stratton, P. M. Clark, and S. D. Luzio
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M. Moriyama, N. Hayashi, C. Ohyabu, M. Mukai, S. Kawano, and S. Kumagai
Performance Evaluation and Cross-Reactivity from Insulin Analogs with the ARCHITECT Insulin Assay,
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