Action of Complexes of the Zinc Group Metals on the Tail Protein of Bacteriophage T2r+

Details Action of Complexes of the Zinc Group Metals on the Tail Protein of Bacteriophage T2r+ Action of Complexes of the Zinc Group Metals on the Tail Protein of Bacteriophage T2r+

Dec 1955

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1955natur.176.1169k&link_type=abstract

Nature, Volume 176, Issue 4494, pp. 1169-1171 (1955).

Computer Science

Scientific paper

A SPECIFIC reaction has been found between complexes of the zinc group metals and the bacterial virus, T2r+. Zinc ions (M/100) do not inactivate T2r+, but if a variety of metal-complexing agents are added to a solution containing zinc nitrate and T2r+, the virus is rapidly and irreversibly inactivated. Identical reactions occur with cadmium ions. Mercuric mercury inactivates T2 as the free ion as well as when present as a complex ion. Cyanide complexes of all three metals and iodide complexes of cadmium and mercuric mercury inactivate the virus. Inactivation also occurs when a number of amino-acids (such as M/100 glycine or glutamic acid) and pure proteins (such as trypsin or chymotrypsin at 2 mgm./ml.) are used as metal-complexing agents. Versene complexes of zinc, cadmium or mercuric mercury do not affect the virus.

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