Labeling of hematoporphyrin with 105Rh and binding studies with human gamma globulin
β Scribed by M.R.A. Pillai; J.M. Lo; D.E. Troutner
- Publisher
- Elsevier Science
- Year
- 1990
- Weight
- 524 KB
- Volume
- 41
- Category
- Article
- ISSN
- 0883-2889
No coin nor oath required. For personal study only.
β¦ Synopsis
Labeling of hematoporphyrin with 105Rh at stoichiometric concentrations is described. Labeling efficiencies of up to 93% could be obtained at pH 9.0 in bicarbonate buffer. Solvent extraction of 105Rh-hematoporphyrin into methyl isobutyl ketone was used to estimate the complex yield. The complex showed high stability and no loss of 105Rh was seen throughout the 6 days of study. 105Rh-hematoporphyrin when incubated with human gamma globulin was seen to be quantitatively bound to the protein. This procedure may be used for labeling monoclonal antibodies with 105Rh for therapeutic applications.
π SIMILAR VOLUMES
The conjugation of a complex formed by reacting RhCl3 with cysteine to human serum albumin has been investigated. Approximately 50% of the rhodium (labeled with 105Rh) was converted to the complex. Conjugation of the complex to HSA via the ECDI method resulted in yields of approximately 40% of the t
An improved electrolytic labeling technique has been developed for tagging human plasma proteins at physiologic pH condition. The basic principle involves the addition of protein after electrolysis and pH adjustment, thus avoiding harsh treatment of the protein and preserving its biological propert