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Physiologic Glycated-Bovine Serum Albumin Determination using Spectrum-UV

  • W. Khoirunnisa
  • , M. I. Nur
  • , S. Widyarti
  • , S. Permana
  • , S. B. Sumitro

Research output: Contribution to journalConference articlepeer-review

Abstract

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.

Original languageEnglish
Article number012003
JournalJournal of Physics: Conference Series
Volume1241
Issue number1
DOIs
Publication statusPublished - 19 Jun 2019
EventInternational Seminar on Bioscience and Biological Education 2018, ISBBE 2018 - Yogyakarta, Indonesia
Duration: 28 Oct 201831 Oct 2018

Keywords

  • Bovine serum albumin
  • glucose
  • glycation
  • UV spectrum

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