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

Henry Wagner Jr., Thomas W. Smith, Michael Young

Research output: Contribution to journalArticle

2 Citations (Scopus)

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 - Jan 1 1974

Fingerprint

Monovalent Cations
Pronase
Digestion
Erythrocytes
Erythrocyte Membrane
Membranes
Membrane Glycoproteins
Ouabain
Adenosine Triphosphatases
Cations
Glycoproteins
Proteins

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

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Resistance of active monovalent cation transport to pronase digestion of intact human erythrocytes. / Wagner Jr., Henry; Smith, Thomas W.; Young, Michael.

In: Archives of Biochemistry and Biophysics, Vol. 163, No. 1, 01.01.1974, p. 95-98.

Research output: Contribution to journalArticle

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