David,
Does this protein you're studying possess any prosthetic groups
(flavin, non-covalent heme, etc.) that could dissociate from the protein
under acidic conditions, and thus result in an observed change in the
protein's 280 nm-absorption?
Bob Keefe
Wadsworth Center/NY State DOH
At 04:36 PM 5/16/2000 -0400, Andrews, David wrote:
>Has anyone ever encountered a protein in which the extinction coefficient
>(or the UV absorbance, if you prefer) was markedly different in the
>denatured versus the native state? I am talking about the absorbance at
>280nm, and I have a protein that, when dissolved in acidic buffers, gives a
>large difference in UV absorbance from its "native" state in non-denaturing
>buffers.
>
>
>David W. Andrews, Ph. D.
>Director, Analytical Research & Development
>BioChem Pharma Inc.
>30 Bearfoot Road
>Northborough, MA 01532
>
>508-351-1004 (voice)
>508-351-9675 (fax)
>
>andrewsd@biochempharma.com
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