Purified bovine colostral IgGIgG
1 was digested by pepsin and rennin, which are predominant milk-clotting enzymes in the abomasus of calf, and each resulting fragment was compared with respect to physicochemical and immunological properties. IgGIgG
1 was digested by rennin for 3hr at 37C mostly at pH3.5 and little at pH5.5. By pepsin IgG was digested appreciably for 1hr at pH4.5 and slightly at pH5.5. Rennin and pepsin digested IgGIgG
1 was separated by gel-filtration through Sephadex G-75, and the molecular weights of the largest fragments, Ren I and Pep I, were both found to be 115, 000 by SDS-polyacrylamide gel-electrophoresis, showing a very similar electrophoretic pattern. Ren I and Pep I contained 5.8 and 5.5 moles of hexose per mole of fragment, respectively. Using rabbit antisera to Ren I and Pep I, the two fragments were shown to be antigenically identical, being probably F (ab')
2.
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