ANTIBODIES AGAINST RESPIRATORY ENZYMES 377 



critical cellular components required for growth and multiplication. 

 (For a comprehensive integration of the genetic relationships of amino 

 acids and the metabolic functions of the dicarboxylic acid system, the 

 reader may be referred to Braunstein, 1947.) 



B. PROBLEMS DEALING WITH THE PRODUCTION OF ANTI- 

 BODY AGAINST THE RESPIRATORY ENZYMES 



In the preceding pages it has been shown that the dehydrogenases 

 so far described contain identical prosthetic groups (coenzyme I or II). 

 Similarly the prosthetic group (riboflavin mononucleotide or riboflavin 

 adenine dinucleotide) of the fiavaproteins, the prosthetic group 

 (adenylic acid) of ■phos-phorylases, the prosthetic group (cocarboxylase, 

 thiamin diphosphate) of carhoxylases, the prosthetic group (iron 

 porphyrin, heme) of the ten diff^erent heme containing enzymes are 

 respectively identical. No matter what the source of these enzymes, 

 the respective prosthetic groups are chemically the same. 



The general question as to whether or not it is possible to produce 

 antibody against the respiratory enzymes evolves into two parts: 



(a) Is it possible to produce antibodies to respiratory enzymes which 

 contain prosthetic groups which are natural to the host? If antibodies 

 are produced, will these react against the prosthetic groups as well as 

 the protein moiety? 



(b) Is it possible to immobilize the activity of the prosthetic groups 

 by combination between the protein component of the enzyme and 

 specific antibody? 



A satisfactory answer to this important biological question requires 

 further critical experimentation. The question as to whether or not 

 the carboxylase-anti-carboxylase combination inactivates carboxylase 

 must be answered.* Does the oxygen combining capacity of hemo- 

 globin in combination with its homologous antibody undergo diminu- 

 tion? Similarly, does the catalase-anticatalase combination produce the 

 inactivation of catalase, etc.? These are questions which must be 

 answered experimentally. The answers will no doubt have direct bear- 

 ing on understanding of the mechanism of immune protection. 



*In collaboration with the author, Drs. V. Z. Pasternak and Ruth E. Miller found 

 that immune sera prepared against isolated yeast carboxylase, or dry whole yeast, or 

 live whole yeast markedly inhibited the activity of the isolated yeast carboxylase (J. 

 Bact., 61, No. 2, 1951). 



