R. J. Collier Ph.D.¹ and A. M. Pappenheimer Jr. Ph.D.¹

¹ From the Biological Laboratories, Harvard University, Cambridge, Massachusetts

It has been demonstrated that low concentrations of highly purified diphtheria toxin specifically inhibit incorporation of labeled amino acids into polypeptides in extracts from HeLa cells and from rabbit reticulocytes. No inhibition of incorporation occurs in the absence of a specific cofactor. This cofactor has been identified as nicotinamide adenine dinucleotide (NAD). It has been shown that it is one of the steps involving transfer of amino acids from soluble ribonucleic acid to the growing polypeptide chain that is affected by the toxin in the presence of NAD.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

• Wykosky, J., Gibo, D. M., Debinski, W. (2007). A novel, potent, and specific ephrinA1-based cytotoxin against EphA2 receptor expressing tumor cells. Molecular Cancer Therapeutics 6: 3208-3218 [Abstract] [Full Text]  
• Pappenheimer, A. M. Jr., Gill, D. M. (1973). Diphtheria: Recent studies have clarified the molecular mechanisms involved in its pathogenesis. Science 182: 353-358  
• Moolten, F. L., Cooperband, S. R. (1970). Selective Destruction of Target Cells by Diphtheria Toxin Conjugated to Antibody Directed against Antigens on the Cells. Science 169: 68-70 [Abstract]  
• Collier, R. J., Cole, H. A. (1969). Diphtheria Toxin Submit Active in vitro. Science 164: 1179-1182 [Abstract]  

Home | Help | Feedback | Subscriptions | Archive | Search

TABLE OF CONTENTS