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American Chemical Society Weekly PressPac -- April 8, 2009

g tests are generally slow, cumbersome, and inaccurate.

In one study, Vern Schramm and Matthew Sturm describe a new test that detects the presence of active ricin in any sample by measuring the release of adenine from specific ricin substrates. Ricin-catalyzed adenine release from ribosomes stops protein synthesis and is the mechanism of action of this deadly toxin. By coupling adenine release to light formation by firefly luciferase, scientists can visualize the presence of ricin by the simple detection of light. The test can detect nanogram (one-billionth of a gram) amounts of ricin in minutes, they note.

In the other, John Barr and Suzanne Kalb describe development of a highly selective three-part test that involves capturing the ricin protein using special antibodies, evaluating the enzymatic activity of the ricin protein by mass spectrometry, and identifying the ricin protein by its amino acid sequence through mass spectrometry. In laboratory tests using small amounts of ricin spiked into food and body fluids, including milk, apple juice, serum, and saliva, the scientists found that the test was highly specific and accurate in comparison to current tests. - MTS

"Detecting Ricin: A Sensitive Luminescent Assay for Ricin A-chain Ribosome Depurination Kinetics"


Vern L. Schramm, Ph.D.
Department of Biochemistry
Albert Einstein College of Medicine of Yeshiva University
Bronx, N.Y. 10461
Phone: 718-430-2813
Fax: 718-430-8565

"Mass Spectrometric Detection of Ricin and its Activity in Food and Clinical Samples"


Contact: Michael Woods
American Chemical Society

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