Synthesis of the Rabbit γG Heavy Chain

  1. Julian B. Fleischman
  1. Departments of Preventive Medicine and Microbiology, Washington University School of Medicine, St. Louis, Missouri

This extract was created in the absence of an abstract.

Excerpt

The finding of variable and common sequences within immunoglobulin polypeptide chains has raised many questions about their genetic and biosynthetic origin. The variable and common parts of the same chain might be coded by separate genes. Information for the two parts could be joined at the DNA level, after transcription of mRNA, or by linking separately synthesized polypeptide chains by a peptide bond. The experiments described here examine this last possibility.

A newly formed polypeptide chain has a gradient of increasing specific activity from the N to the C terminal following incorporation of radioactive amino acids (Dintzis, 1961). If an immunoglobulin polypeptide chain were synthesized as a single chain, it would contain a single specific activity gradient from the N to the C terminal. However, if the variable and common parts of the chain were synthesized separately and simultaneously, the completed chain would contain two such gradients, one corresponding to...

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