A comparative study of the interaction of Myocrisin with albumin and γ-globulin

• Published in: Journal of pharmaceutical and biomedical analysis Vol. 13; no. 2; pp. 99 - 102
• Main Authors: McDonald, C., Mortimer, P., McAllister, G., Gardiner, P.E., Reglinski, J., Smith, W.E.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01.02.1995; Elsevier Science
• Subjects: albumin; Analysis; Binding Sites; Biological and medical sciences; gamma-Globulins - metabolism; General pharmacology; Gold; Gold - metabolism; Gold Sodium Thiomalate - metabolism; Gold Sodium Thiomalate - pharmacology; Medical sciences; Myocrisin; Pharmacology. Drug treatments; Protein Binding; Serum Albumin - metabolism; γ-globulin; Gold; γ-globulin; albumin; Myocrisin; Proteins; Biological fixation; Gold Compounds; Albumin; Gel filtration; Antirheumatic agent; Globulin γ; In vitro; Quantitative analysis; Atomic absorption spectrometry
• ISSN: 0731-7085; 1873-264X
• DOI: 10.1016/0731-7085(94)00118-L

The reactions of Myocrisin with albumin and γ-globulin have been investigated using atomic absorption spectrometry and gel filtration. Albumin rapidly binds gold up to the levels predicted from the concentration of free sulphydryl groups present in the protein. However, in the presence of glutathione, gold incorporation is increased, suggesting that in vivo, free thiols (glutathione, thiomalate) may facilitate gold uptake by the protein. In comparison, γ-globulin is found to be capable of binding up to one atom of gold per molecule of protein in a slow reaction which requires high Myocrisin concentrations.