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Dear Dr Wulkan, I do not presume to be an expert on this phenomemon, nor do I wish to denounce the opinions of learned colleagues, but, I would not be in a hurry to jump to conclusions. Urea is a powerful dissociator of proteins (second only to Clelland's Reagent, in my opinion), and it can often behave (in vivo), in an unpredictable manner. Obviously, I am not familiar with your precise reference ranges for Urea, but I would imagine that we are talking about an approximate 10-fold increase -- certainly enough to cause problems. I would be very interested in receiving a sample from this patient for further investigation. Sincerely, Dr David E Bevan American Mission Hospital PO Box 1 Manama BAHRAIN Tel: +973 9605014 Fax:: +973 234194 ----- Original Message ----- From: R.W. Wulkan To: [log in to unmask] Cc: [log in to unmask] Sent: Thursday, September 09, 1999 10:57 AM Subject: Albumin Dubliners Dear collegue, Yesterday, I was called to inspect an unusual protein electrophoresis pattern. One lane of the Paragon gel showed an broad albumin band, "bearding" towards the anode, no extra (prealbumin) band to be seen. The patient turned out to have a chronic renal failure: kreat 480 umol/L, urea 63 mmol/L, anion gap 24 mEq/L. Our present theory is that the broadening is caused by association of albumin with charged molecules, retained by severe renal failure. The patient did not get albumin therapy. Is there anyone familiar with this phenomenon? The only bearding band known to us thus far are the Dubliners, so we propose the name albumin Dubliners. Best wishes Raymond Wulkan Zuiderziekenhuis Rotterdam The Netherlands