Resistance of active monovalent cation transport to pronase digestion of intact human erythrocytes

Henry Wagner, Thomas W. Smith, Michael Young

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Human erythrocytes were treated with pronase under conditions which gave complete cleavage of the pronase-sensitive major protein and glycoprotein components of the membrane. 86Rb+ influx of these modified cells did not differ significantly from that of untreated cells, and showed identical sensitivity to inhibition by ouabain. Pronase treatment of porous erythrocyte ghost membranes resulted in complete loss of (Na+ + K+)-ATPase activity. These results indicate that the cation-transport complex is not readily accessible from the outer surface of native intact membranes.

Original languageEnglish (US)
Pages (from-to)95-98
Number of pages4
JournalArchives of Biochemistry and Biophysics
Volume163
Issue number1
DOIs
StatePublished - Jul 1974

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Resistance of active monovalent cation transport to pronase digestion of intact human erythrocytes'. Together they form a unique fingerprint.

  • Cite this