Modifying effects of carboxyl group on the interaction of recombinant S100A8/A9 complex with tyrosinase

详细信息    查看全文

• 作者：Fatemeh NematiNiko^a ; Koorosh Goodarzvand Chegini^b ; Hamideh Asghari^c ; Abbas Amini^d ; ^{a.amini@westernsydney.edu.au} ; Nematollah Gheibi^e ; ^{ngheibi@qums.ac.ir}
• 关键词：MT ; mushroom tyrosinase ; L-DOPA ; L-3 ; 4-dihydroxyphenylalanine ; DOPA ; 3 ; 4-dihydroxyphenyl alanine ; r ; recombinant ; PPI ; protein-protein interaction ; CD ; circular dichroism spectroscopy ; NMR ; nuclear magnetic resonance ; WRK ; Woodward's reagent K ; UV-CD ; far ultraviolet circular dichroism spectrum ; IPTG ; isopropyl β-D-1-thiogalactopyranoside ; ANS ; anilinonaphthalene-8-sulfonic acid ; SDS-PAGE ; Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis ; PBS ; phosphate buffered solutions.
• 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：1865
• 期：3
• 页码：370-379
• 全文大小：1611 K
• 卷排序：1865

文摘

Incubation of WRK with S100A8/A9 causes conformational changes in the protein. Modification in S100A8/A9 results in increasing the tyrosinase activity. Recombinant S100A8/A9 complex has ability to decrease tyrosinase activity. Tyrosinase inner hydrophobic regions have interaction with S100A8/A9.