Analysis of differential protein expression in Acidithiobacillus ferrooxidans grown under different energy resources respectively using SELDI-ProteinChip technologies.
Surface-enhanced laser desorption/ionization (SELDI)-time of flight is an affinity-based mass spectrometric method in which proteins of interest are selectively absorbed to a chemically modified surface on a chip, which allows proteomic analysis with limited material requirements. This characteristic makes it a valuable technique for microbiologists handling problematic samples, such as low cell number cultures. In this study, we explored differential-expressed proteome of Acidithiobacillus ferrooxidans cultivated with Fe(2+) and elemental sulfur separately by adopting the protein biochip SELDI approach. The cell lysates of A. ferrooxidans were applied onto Ciphergen ProteinChip WCX2, SAX2 and IMAC-Cu arrays. Proteins bound to the chips were analyzed on a ProteinChip Reader Model PBS II. A summary of the molecular masses of the differentially regulated proteins found on WCX2, IMAC-Cu and SAX2 was obtained and 28 differentially expressed proteins were found on the molecular weight range of 5.0 to 25 kDa.
He
Zhiguo
Z
School of Resources Processing and Bioengineering, Central South University, Changsha, Hunan Province, 410083 PR China.
Zhong
Hui
H
Hu
Yuehua
Y
Xiao
Shengmu
S
Xu
Jin
J
D042763:Acidithiobacillus / Q000737:chemistry / Q000254:growth & development / Q000378:metabolism*; D001426:Bacterial Proteins / Q000032:analysis / Q000096:biosynthesis*; D007501:Iron / Q000378:metabolism; D040081:Protein Array Analysis / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D013455:Sulfur / Q000378:metabolism
D001426:Bacterial Proteins; D013455:Sulfur; D007501:Iron