Fractionation of Bence-Jones protein by starch gel electrophoresis.
نویسندگان
چکیده
The development by Smithies (1955a) of starch gel as a medium for the electrophoresis of protein material marked an important advance, as it combines separation by electrical mobility with a form of pore filtration. Smithies (1955b) has been able to obtain 12 or more protein fractions from human serum with his one-dimensional technique and equally remarkable separation has been obtained with animal sera (Ashton, 1957 ; Latner and Zaki, 1957). Applying this technique to the study of the abnormal proteins of multiple myeloma, BenceJones protein, which behaves as a single entity on paper electrophoresis, can often be resolved into two or more components in starch gel. There are a few reports in the literature of the occurrence of more than one abnormal electrophoretic fraction in the urine (Putnam and Stelos, 1953; Soulier, 1953; Wunderley and Caspani, 1954; ten Thije, 1956; Vis and Crokaert, 1956; Cummings, 1957; Gobert-Jones, 1957; Owen, 1957; Woodliff, Ainsworth, and Flemans, 1958). However, most electrophoretic studies have shown only a single abnormal protein, with or without albumin and normal serum globulins (Gutman, Moore, Gutman, McClellan, and Kabat, 1941; Moore, Kabat, and Gutman, 1943; Rundles, Cooper, and Willett, 1951 ; Slater and Kunkel, 1953; Osserman and Lawlor, 1955; Owen and Rider, 1957). The findings on 13 urines from cases of multiple myeloma, eight of which showed the classical heat reactions of Bence-Jones protein, are reported here.
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ورودعنوان ژورنال:
- Journal of clinical pathology
دوره 11 4 شماره
صفحات -
تاریخ انتشار 1958