2-Mercaptoethylamine fragments

Figure 1.77 Disulfide reducing agents such as 2-mercaptoethylamine can be used to cleave the disulfide bonds in the hinge region of antibody molecules. Either intact IgG molecules or F(ab )2 fragments may be reduced in this manner to yield monofunctional antigen binding fragments.

The actual pathway by which fatty acid oxidation occurred was established by Lynen (1952-1953). Its unique and characteristic reaction was the thioclastic attack by coenzyme A on the B-ketoacyl CoA derivative, splitting off the 2C fragment, acetyl CoA. Free coenzyme A was very difficult to isolate and although it was synthesized in Todd s laboratory in Cambridge in the mid-1950s, much of the early work from Lynen s laboratory utilized A-acetyl cysteamine as a not very efficient (ca.1%) coenzyme A analogue. It carried the essential thiol group of the B-mercaptoethylamine end of CoA and could be used in most, but not all, of the steps in the spiral. 

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