Analysis of Cibacron blue F3G-A interaction with therapeutic proteins by MALDI-TOF mass spectrometry.
The formation of the complexes between Cibacron blue F3G-A and two therapeutic proteins, recombinant human interferon-alpha2b and recombinant human growth hormone, was investigated. The method of time-resolved limited proteolysis coupled with MALDI-TOF mass spectrometry was used. The analysis of peptide maps revealed that A(17)HR(19) and L(20)HQLAFDTYQEFEEAYIPK(38) of hGH, and R(14)TLMLLAQMR(23) and D(33)RHDFGFPQEEFGNQFQK(50) of hIFN-alpha2b, exhibit affinity to Cibacron blue F3G-A.
Department of Chemistry and Bioengineering, Vilnius Gediminas Technical University, Vilnius, Lithuania.
Ieva
I
Sutkeviciute
Jolanta
J
Sereikaite
Vladas-Algirdas
VA
Bumelis
D004396:Coloring Agents / Q000737:chemistry*; D004347:Drug Interactions; D019382:Human Growth Hormone / Q000737:chemistry*; D006801:Humans; D000077190:Interferon alpha-2; D016898:Interferon-alpha / Q000737:chemistry*; D008024:Ligands; D010455:Peptides / Q000737:chemistry*; D011994:Recombinant Proteins; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D014227:Triazines / Q000737:chemistry*
D004396:Coloring Agents; D000077190:Interferon alpha-2; D016898:Interferon-alpha; D008024:Ligands; D010455:Peptides; D011994:Recombinant Proteins; D014227:Triazines; D019382:Human Growth Hormone; C012842:Cibacron Blue F 3GA