Preparation of a gelatin-binding conjugate containing gold thiomalate.
Plasma fibronectin has a range of binding sites, for ligands, including denaturated collagen (gelatin). It has been proposed that this activity may be used for nonimmune drug targeting to sites in the extra-cellular matrix such as the targeting of gold thiomalate to rheumatoid joints. In the present study, a novel conjugate has been developed, consisting of the gold thiomalate bound at high density to the gelatin-binding domain of fibronectin, through a polylysine carrier. Isolation and cross-linking of suitable fragments of fibronectin (relative molecular weights 65 and 52 kDa) to polylysine is followed by conjugation to gold thiomalate on a solid phase, gelatin-agarose affinity absorbent. Although gold thiomalate has the ability to inactivate, the protein-gold conjugate produced by this technique retained its gelatin-binding activity.
Brown
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RA
Institute of Orthopaedics (University College London), Royal National Orthopaedic Hospital Trust, U.K.
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Ejim
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D004337:Drug Carriers; D004591:Electrophoresis, Polyacrylamide Gel; D005353:Fibronectins / Q000737:chemistry / Q000302:isolation & purification; D005780:Gelatin / Q000737:chemistry; D006052:Gold Sodium Thiomalate / Q000008:administration & dosage* / Q000737:chemistry; D006801:Humans; D006868:Hydrolysis; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D011107:Polylysine; D011485:Protein Binding; D014357:Trypsin
D004337:Drug Carriers; D005353:Fibronectins; D010446:Peptide Fragments; D006052:Gold Sodium Thiomalate; D011107:Polylysine; D005780:Gelatin; D014357:Trypsin