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The Journal of Cell Biology, Vol 76, Issue 2 323-340, Copyright © 1978 by The Rockefeller University Press

JOURNAL ARTICLE

Secretion granules of the rabbit parotid. Selective removal of secretory contaminants from granule membranes

J. D. Castle and G. E. Palade
Section of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.

A membrane subfraction obtained from secretion granules isolated from rabbit parotid has been shown to be contaminated by residual secretory proteins to an estimated level of 25-30% of its total protein. In the present study an additional contaminant has been identified by improved mixing experiments and by comparative peptide mapping of specific polypeptides recovered from gels of membrane and content subfractions. This contaminant coelectrophoresis with (and probably comprises the bulk of) the majority component of the membrane subfraction (mol wt approximately 40,000). The contaminating polypeptides can be removed to a large extent by treating the membranes with low concentrations of saponin in the presence of 0.3 M Na2SO4. Although this treatment disrupts the typical bilayer structure of the granule membrane, it does not appear to cause dissociation of its phospholipids or bona fide membrane proteins.
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