E. Suhartono, I. Thalib, I. Aflanie, Z. Noor, R. Idroes
This study aims to explain the interaction of cadmium (Cd) with serum albumin through visible light (UV-Vis) spectroscopy approach. This study is an in vitro experimental study using Cd with several concentrations and Bovine Serum Albumin (BSA). Each solution was then incubated for 10 min at 37°C, and measured the absorbance at 220-300 nm. The absorbance data is then presented in graphical form. From the graph, a linear equation will appear to calculate the value of metal binding constants (K) to proteins. Also, in this present study we analsyed the ratio between A220 and A220 to identify changes in the protein region especially tyrosine and peptide bonds. The results show that the addition of Cd in different concentrations could increase the absorbance with a constant value (K) = 1.634. Based on the result, it seems the addition of Cd in different concentrations will lead the reaction to form BSA-Cd. Also, the result shows that the ration of A220/A280 were decreased with the increasing of Cd concentration. In conclusion, the addition of Cd could interact and changes the protein structure in BSA. © Published under licence by IOP Publishing Ltd.
Department of Medical Chemistry/Biochemistry, Faculty of Medicine, Lambung Mangkurat University, South Kalimantan, Banjarmasin, 70712, Indonesia; Research and Development Unit, Mutiara Bunda Mother and Child Hospital, Martapura, South Kalimantan, 70614, Indonesia; Department of Forensic, Faculty of Medicine, Lambung Mangkurat University, South Kalimantan, Banjarmasin, 70232, Indonesia; Department of Orthopaedic Surgery, Faculty of Medicine, Lambung Mangkurat University, South Kalimantan, Banjarmasin, Indonesia; Department of Chemistry/Pharmacy, Faculty of Mathematics and Natural Sciences, Syiah Kuala University, Aceh, 24415, Indonesia
Research at a Glance
Register to unlock
Topics & SDG Alignment
Register to unlock
Collaboration
Register to unlock
Author Profile (Selected)
Register to unlock
References Overview
Register to unlock
Journal & Source
Register to unlock
Metadata & Integrity
Register to unlock