Open AccessPhysiologic Glycated-Bovine Serum Albumin Determination using Spectrum-UV
Author(s) -
Wulida Khoirunnisa,
Moch Nur,
Sri Widyarti,
Sofy Permana,
Sutiman Bambang Sumitro
Publication year - 2019
Publication title -
journal of physics. conference series
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.21
H-Index - 85
eISSN - 1742-6596
pISSN - 1742-6588
DOI - 10.1088/1742-6596/1241/1/012003
Subject(s) - glycation , bovine serum albumin , chemistry , chromatography , albumin , serum albumin , glycosylation , incubation , sugar , reducing sugar , biochemistry , receptor
Albumin is not native phase, but it physiologically-binding with another compound which conclude the functions as transporter and scavenger. The general non-enzymatic reaction within proteins, which has a significant impact on their physical and functional properties by reducing sugar, known as glycation. The study investigated the effective composition to glycate the bovine serum albumin (BSA) by UV-spectrum. Five BSA concentrations (750, 500, 100, 10 and 1 mM) was prepared in PBS pH 7.4. The glycation carried out using glucose concentrations (2M, 1.5 M, 1 M, 500 mM, and 100 mM) before and after incubation for seven days. Depending on concentration, BSA 1 mM and 10 mM showed the best UV spectrum of protein that two peaks, 220 and 280 nm. Hence, the glycation by high concentration of glucose would be made a conformational change of BSA which is marked by the UV-spectrum of BSA configuration. Glucose 100 and 500 mM was effective to glycate BSA.