RE: Stainless steel systems (fwd)

bcdchin@muccmail.missouri.edu
Tue, 28 Jul 98 10:21:00 CST

It is my understanding as stated below that the contact surface area of the
frits is an excellent place to catch or inactivate proteins such as
phosphoproteins and kinases. The nitric acid trick is to clean and passivate
the SS for resistance to corrosion. Overnight EDTA treatment can be used to
passivate the SS for lesson the chances of P-proteins sticking and the leaching
of metals from the SS.

The SS frits can easily be replaced with plastic ones from various vendor such
as Upchurch.

No company endorsement is given nor implied.

David T. Chin
Director, Protein Core
Univ. of Missouri - Columbia
Columbia, MO 65211

NEW ADDRESS:
2-17 Agriculture Building (office)
2-31 Agriculture Building (Lab)

e-Mail: chind@missouri.edu
web: http:\\www.missouri.edu\~pc
[mailto:chind@missouri.edu]
Phone: 573-882-2027
Fax: 573-882-7105

-----Original Message-----
From: Ombudsman account for AECOM <ombudsmn@aecom.yu.edu> at MU-Internet

Sent: Tuesday, July 28, 1998 10:00 AM
To: abrf@aecom.yu.edu at MU-Internet
Subject: Stainless steel systems (fwd)

I worked at a chromatography company earlier in my career. We tested
stainless steel for proteins and peptides and found that the tubing made
very little difference. However, we found that the column frits made a
lot of difference. In retrospect that makes sense. There is a lot more
surface area exposed in the frit than by the tubing. What was even more
interesting was that passivated stainless steel (washed with nitric
acid) performed more poorly (i.e., absorbed more protein) than "dirty"
stainless. We also found that the amount of protein absorption was
strongly dependent upon the protein.