Labeling of human serum albumin with 105Rh-cysteine complexes.
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 total rhodium or approximately 80% of the Rh-cysteine complex. No conjugation was observed in the absence of the ECDI. At approximately equal molar concentrations of rhodium and HSA, an average of approximately 0.4 rhodium atoms per HSA molecule was achieved.
Lo
J M
JM
Department of Chemistry, University of Missouri, Columbia 65211.
Pillai
M R
MR
John
C S
CS
Troutner
D E
DE
D003545:Cysteine; D006801:Humans; D007553:Isotope Labeling / Q000379:methods*; D009942:Organometallic Compounds; D012238:Rhodium; D012709:Serum Albumin
D009942:Organometallic Compounds; D012709:Serum Albumin; D012238:Rhodium; D003545:Cysteine