Hello,
I am trying to isolate a protein who has a cysteine rersidue. I am testing if this cysteine is making a disulfide bond with another monomer as a mode of regulation. I found a paper who was saying that proetins redox state can be fixed by pption with TCA but it doe snot give a detailed protocol plus they work on E.c oli while i am working on bacillus. so anyone could help me what to do exactly? Thank you in advance.
ali
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nitha
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Posted 16 August 2004 - 04:23 AM
aloks321, on Jul 21 2004, 03:08 PM, said:
Hello,
I am trying to isolate a protein who has a cysteine rersidue. I am testing if this cysteine is making a disulfide bond with another monomer as a mode of regulation. I found a paper who was saying that proetins redox state can be fixed by pption with TCA but it doe snot give a detailed protocol plus they work on E.c oli while i am working on bacillus. so anyone could help me what to do exactly? Thank you in advance.
ali
I am trying to isolate a protein who has a cysteine rersidue. I am testing if this cysteine is making a disulfide bond with another monomer as a mode of regulation. I found a paper who was saying that proetins redox state can be fixed by pption with TCA but it doe snot give a detailed protocol plus they work on E.c oli while i am working on bacillus. so anyone could help me what to do exactly? Thank you in advance.
ali
i would like to know the principle behind TCA precipitation of proteins.when some enzymes like trypsin with its substrate,say,casein is allowed to react to each other for some time and then those were
precipitated by 12.5% TCA what will be there in the supernatent?
