Solution- and Crystal-Phase Covalent Modification of Lysozyme by a Purpose-Designed Organoruthenium Complex. A MALDI-TOF MS Study of its Metal Binding Sites

ChemBioChem ◽  
2003 ◽  
Vol 5 (1) ◽  
pp. 99-109 ◽  
Author(s):  
Michèle Salmain ◽  
Bertrand Caro ◽  
Françoise Le Guen-Robin ◽  
Jean-Claude Blais ◽  
Gérard Jaouen
Keyword(s):  
Metal Binding ◽  
Binding Sites ◽  
Covalent Modification ◽  
Crystal Phase ◽  
Maldi Tof Ms ◽  
Metal Binding Sites ◽  
Maldi Tof ◽  
Tof Ms

scholarly journals A novel mechanism of “metal gel-shift” by histidine-rich Ni2+-binding Hpn protein from Helicobacter pylori strain SS1

2016 ◽  
Author(s):  
Rahul Mahadev Shelake ◽  
Yuki Ito ◽  
Junya Masumoto ◽  
Eugene Hayato Morita ◽  
Hidenori Hayashi
Keyword(s):  
Helicobacter Pylori ◽  
Metal Binding ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Metal Species ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Sds Page ◽  
Gel Shift ◽  
Tof Ms

AbstractSodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) is a universally used method for determining approximate molecular weight (MW) in protein research. Migration of protein that does not correlate with formula MW, termed “gel shifting” appears to be common for histidine-rich proteins but not yet studied in detail. We investigated “gel shifting” in Ni2+-binding histidine-rich Hpn protein cloned from Helicobacter pylori strain SS1. Our data demonstrate two important factors determining “gel shifting” of Hpn, polyacrylamide-gel concentration and metal binding. Higher polyacrylamide-gel concentrations resulted in faster Hpn migration. Irrespective of polyacrylamide-gel concentration, preserved Hpn-Ni2+ complex migrated faster (3-4 kDa) than apo-Hpn, phenomenon termed “metal gel-shift” demonstrating an intimate link between Ni2+ binding and “gel shifting”. To examine this discrepancy, eluted samples from corresponding spots on SDS-gel were analyzed by matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF-MS). The MW of all samples was the same (6945.66±0.34 Da) and identical to formula MW with or without added mass of Ni2+. MALDI-TOF-MS of Ni2+-treated Hpn revealed that monomer bound up to six Ni2+ ions non-cooperatively, and equilibrium between protein-metal species was reliant on Ni2+ availability. This corroborates with gradually increased heterogeneity of apo-Hpn band followed by compact "metal-gel shift" band on SDS-PAGE. In view of presented data metal-binding and “metal-gel shift” models are discussed.

Identification of metal-binding to proteins in seed samples using RF-HPLC-UV, GFAAS and MALDI-TOF-MS

2016 ◽  
Vol 211 ◽  
pp. 910-915 ◽  
Author(s):  
Leila M.B. Rigueira ◽  
Diogo A.P.D. Lana ◽  
Daniel M. dos Santos ◽  
Adriano M. Pimenta ◽  
Rodinei Augusti ◽  
...  
Keyword(s):  
Metal Binding ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Tof Ms

895: Proteomic Analysis of Sera from Bladder Cancer Patients with MALDI-TOF-MS

2007 ◽  
Vol 177 (4S) ◽  
pp. 297-297
Author(s):  
Kristina Schwamborn ◽  
Rene Krieg ◽  
Ruth Knüchel-Clarke ◽  
Joachim Grosse ◽  
Gerhard Jakse
Keyword(s):  
Bladder Cancer ◽  
Cancer Patients ◽  
Proteomic Analysis ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Tof Ms

HPTLC-MALDI/TOF/MS vs. HPLC-ESI/MS2 for identification to flavonoids in plant extracts

Planta Medica ◽  
2016 ◽  
Vol 81 (S 01) ◽  
pp. S1-S381
Author(s):  
L Fougère ◽  
D Da Silva ◽  
E Destandau ◽  
C Elfakir
Keyword(s):  
Plant Extracts ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Tof Ms

Infektionserreger beim Schwein – Analyse des kultivierbaren Mikrobioms mittels MALDI-TOF MS

2017 ◽  
Author(s):  
M Erhard ◽  
M Metzner ◽  
D Köhler-Repp ◽  
B Köhler ◽  
R Storandt
Keyword(s):  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Tof Ms

Quantitative metabolomics of Iranian saffron based on their HPLC-DAD and MALDI-TOF-MS

2019 ◽  
Author(s):  
M Hooshyari ◽  
H Rezadoost ◽  
P Ghezellou ◽  
A Ghassempour
Keyword(s):  
Maldi Tof Ms ◽  
Quantitative Metabolomics ◽  
Maldi Tof ◽  
Tof Ms
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