Abstract
Diethylenetriaminepentaacetic acid (DTPA), a strong chelating agent, was covalently linked to murine monoclonal anti-HLA IgG1 antibody (H-1) with the use of poly(l-lysine) (Mr 14 000) as a multivalent, intermediary carrier, via thiol-disulfide exchange reaction. The conjugates contained up to 42.5 mol DTPA per mol antibody, and retained over 90% of their antibody activity in vitro. The conjugates incorporated gadolinium (Gd) through an exchange reaction with Gd-EDTA, used to prevent colloid formation and nonspecific binding of the free metal. The IgG-poly(l-lysine)-DTPA-Gd had a greater effect per mol on proton relaxation rates than DTPA-Gd itself. Use of poly(l-lysine) as an intermediary carrier for attachment of chelating agents to IgG thus offers great potential for achieving high-specific-activity conjugates, particularly for use as biologically specific contrast agents in nuclear magnetic resonance imaging.
| Original language | American English |
|---|---|
| Pages (from-to) | 460-467 |
| Number of pages | 8 |
| Journal | BBA - General Subjects |
| Volume | 883 |
| Issue number | 3 |
| DOIs | |
| State | Published - Oct 1 1986 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
Keywords
- Diethylenetriaminepentaacetic acid
- Gadolinium
- Immunoglobulin conjugate
- Monoclonal antibody
- Poly(l-lysine)
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