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Science 3 May 1968:
Vol. 160. no. 3827, pp. 538 - 539
DOI: 10.1126/science.160.3827.538
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Articles

Plasma 3S ggr1-Globulin: Identity with Erythrocyte Carbonic Anhydrase B

David Gitlin 1, Mary Boesman 1, Karl Schmid 1, and Pekka Vuopio 1

1 University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, and Boston University School of Medicine, Boston, Massachusetts

The 3S ggr1, 2S ggr2, and 0.5S ggr2 fractions of human plasma are heterogeneous in protein composition. Although each fraction contained a relatively small amount of protein antigenically related to the immunoglobulin light chains, most of the proteins were unrelated to immunogloublin G or its light chains. Of the 3S ggr1-globulins the greater part was immunochemically identical to carbonic anhydrase B and had carbonic anhydrase activity. These findings explain earlier reports of an immunochemical similarity between 3S ggr1-globulins and immunoglobulin light chains in spite of marked differences in amino acid and peptide composition between the two. Apparently not all plasma ggr-globulins are necessarily immunoglobulins.

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Science. ISSN 0036-8075 (print), 1095-9203 (online)