In:
Canadian Journal of Biochemistry, Canadian Science Publishing, Vol. 45, No. 2 ( 1967-02-01), p. 203-211
Abstract:
DEAE-Sephadex chromatography was employed to fractionate the γA globulins of normal and A-myeloma human sera. By immunoelectrophoresis, the normal γA globulins had mobilities ranging from that of γ 1 to α 2 globulins, whereas the myeloma γA globulins were of essentially uniform mobility. Most of the normal γA globulins were homogeneous with respect to sedimentation in a sucrose density gradient, indicating that their immunoelectrophoretic heterogeneity was due largely to differences in molecular charge rather than size.
Type of Medium:
Online Resource
ISSN:
0008-4018
Language:
English
Publisher:
Canadian Science Publishing
Publication Date:
1967