Proteolytic dissection

Yao, X., Aeonso, C., Fenselau, C. (2003). Dissection of proteolytic 180 labeling endoprotease-catalyzed 160-to-180 exchange of truncated peptide substrates./. Proteome Res. 2, 147-152. 

Dissection of Multifunctional Molecules. Protein molecules generally have more than one antigenic site and occasionally more than one distinctly diflFerent biologically active site. Whenever these sites are discretely separated spatially and are joined by only one or a few interconnecting peptide chains, proteolytic enzymes may separate the sites whil preserving biological activities. Proteolytic scission is most successful when the molecule is elongated or composed of more than one polypeptide chain. 

Proteolytic dissection has contributed substantially to our knowledge of the structure and function of the y-globulins. The yG-immunoglobulins constitute the largest portion, about 80% or more, of the y-globulin system and have MW of about 160,000. The molecules are elongated, about 235 X 44 A. A major advance in understanding the structure and... 

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