Heterogeneity of the sialoglycoproteins of the normal human erythrocyte membrane

Mueller, T.J.; Dow, A.W.; Morrison, M.

Biochemical and Biophysical Research Communications 72(1): 94-99

1976


ISSN/ISBN: 0006-291X
PMID: 985486
DOI: 10.1016/0006-291x(76)90965-7
Accession: 005566475

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Abstract
The sialoglycoproteins of the human erythrocyte membrane can be separated into at least 8 periodic acid Schiff-positive components using sodium dodecyl sulfate gel electrophoresis in the discontinuous buffer system of Laemmli. All 8 components can also be labeled by mild periodate oxidation followed by reduction with NaB3H4. Periodic acid Schiff 2 can be resolved into at least 3 distinct components. Two sialoglycoproteins, with apparent MW of 35,000 and 27,000 were not labeled by lactoperoxidase-catalyzed iodination at the external membrane surface.