Hostname: page-component-848d4c4894-xfwgj Total loading time: 0 Render date: 2024-06-26T00:27:19.498Z Has data issue: false hasContentIssue false
  • English
  • Français

Direct and indirect actions of radiation on viruses and enzymes

Published online by Cambridge University Press:  06 April 2009

Douglas Lea ,
Kenneth M. Smith ,
Barbara Holmes  and
Roy Markham
Douglas Lea
Affiliation:
Strangeways Laboratory, Plant Virus Research Station, Biochemical Laboratory, and Molteno Institute, Cambridge
Kenneth M. Smith
Affiliation:
Strangeways Laboratory, Plant Virus Research Station, Biochemical Laboratory, and Molteno Institute, Cambridge
Barbara Holmes
Affiliation:
Strangeways Laboratory, Plant Virus Research Station, Biochemical Laboratory, and Molteno Institute, Cambridge
Roy Markham
Affiliation:
Strangeways Laboratory, Plant Virus Research Station, Biochemical Laboratory, and Molteno Institute, Cambridge
Get access Rights & Permissions [Opens in a new window]

Extract

1. The inactivation by γ-rays of tobacco mosaic virus is studied at various concentrations. It is found that the inactivation dose is independent of concentration at high concentrations, and at low concentrations also attains a constant, but lower, value. Over an intermediate range the inactivation dose increases with increase of concentration.

2. These facts are explained on the basis that when irradiated dry or in concentrated solution the inactivation is direct and due to ionization produced inside the virus particle. At lower concentrations the inactivation is largely indirect and due to ionization of the water.

3. Gelatin added to the solution protects the virus against the indirect action of radiation.

4. Curves are given of the inactivation of dry preparations of ribonuclease and adenylpyro-phosphatase (myosin) by X-rays.

5. It is shown that on the assumption that a single ionization in an enzyme molecule leads to its inactivation, measurement of the inactivation dose leads to a rough estimate of the molecular weight of the enzyme.

6. There appears to be no fundamental difference in the mechanism of radiation-inactivation of viruses and enzymes.

All irradiations were carried out at the Strangeways Laboratory. The virus was prepared and tested at the Plant Virus Station and the Molteno Institute. The enzymes were prepared and estimated at the Biochemical Laboratory. We are indebted to the British Empire Cancer Campaign for defraying the cost of the X-ray equipment at the Strangeways Laboratory.

Type
Research Article
Information
Parasitology , Volume 36 , Issue 1-2 , September 1944 , pp. 110 - 118
Copyright
Copyright © Cambridge University Press 1944

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Bailey, K. (1942). Biochem. J. 36, 121.Google Scholar
Beidgman, W. B. & Williams, J. W. (1942). Ann. N.Y. Acad. Sci. 43, 195.Google Scholar
Dale, W. M. (1940). Biochem. J. 34, 1367.Google Scholar
Dale, W. M. (1942). Biochem. J. 36, 80.Google Scholar
Dale, W. M., Meredith, W. J. & Tweedie, M. C. K. (1943). Nature, Lond., 151, 281.Google Scholar
Exner, F. M. & Luria, S. E. (1941). Science, 94, 394.Google Scholar
Fricke, H. (1934). Cold Spr. Harb. Symp. 2, 241.Google Scholar
Fricke, H., Hart, E. J. & Smith, H. P. (1938). Chem. Phys, 6, 229.Google Scholar
Friedewald, W. F. & Anderson, R. S. (1940). Proc. Soc. Exp. Biol., N.Y., 45, 713.Google Scholar
Friedewald, W. F. & Anderson, R. S. (1941). J. Exp. Med. 74, 463.Google Scholar
Gowen, J. W. (1940). Proc. Nat. Acad. Sci., Wash., 26, 8.Google Scholar
Kunitz, M. (1941). J. Gen. Physiol. 24, 15.Google Scholar
Lea, D. E. (1940 a). J. Genet. 39, 181.Google Scholar
Lea, D. E. (1940 b). Nature, Lond., 146, 137.Google Scholar
Lea, D. E. (1941). Amer. J. Roentg. 45, 614.Google Scholar
Lea, D. E. & Salaman, M. H. (1941). Brit. J. Exp. Path. 23, 27.Google Scholar
Lea, D. E. & Smith, K. M. (1940). Parasitology, 32, 405.Google Scholar
Lea, D. E. & Smith, K. M. (1942). Parasitology, 34, 227.Google Scholar
Luria, S. E. & Exner, F. M. (1941). Proc. Nat. Acad. Sci., Wash., 27, 370.Google Scholar
Needham, D. M. (1942). Biochem. J. 36, 113.Google Scholar
Neurath, H. (1942). Chem. Rev. 30, 357.Google Scholar
Rothen, A. (1942). Ann. N.Y. Acad. Sci. 43, 229.Google Scholar
Svedberg, T. & Pedersen, K. O. (1940). The Ultracentrifuge p. 414. Oxford.Google Scholar
Syverton, J. T., Berry, G. P. & Warren, S. L. (1941). J. Exp. Med. 74, 223.Google Scholar
Wollman, E. & Lacassagne, A. (1940). Ann. Inst, Pasteur, 64, 5.Google Scholar
Wollman, E., Holweck, F. & Luria, S. E. (1940). Nature, Lond., 145, 935.Google Scholar