Chemistry and Biology of Alpha 2-Macroglobulin,
NEW YORK ACADEMY OF SCIENCES NY
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Only a few years ago, alpha 2-macroglobulin alpha 2 M was a rather mysterious protein and its behavior appeared to have little in common with that of other systems in biochemistry. Recently, however, our understanding of the chemistry of alpha 2 M has developed dramatically. The determination of the complete primary structure, which was presented at this conference for the first time, is a rather striking indication of this advance. At the same time, the confluence of several diverse lines of research has made the chemistry and biology of alpha 2 M of more general interest to biomedical science. The unexpected homology between alpha 2-M and the complement proteins C3 and C4 and the discovery of a unique new configuration of amino acids, the thiolester, have simultaneously opened a new field of protein chemistry and enlarged our view of the general area of nucleophilic reactions at peptide centers. Our increased understanding of the role of alpha 2 M in the clearance of proteases and the possibly fortuitous use of alpha 2 M as a probe for receptor-mediated endocytosis have, likewise, expanded our horizons in this area of chemistry and physiology.