Spontaneous and enzyme-induced dimer formation and its role in membrane permeability II. The mechanism of movement of glycerol across the human erythrocyte membrane

W. D. Stein*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

1. 1. Kinetic studies of the rate of penetration of glycerol across the membrane of the human red blood cell suggest that this does not occur by simple diffusion. 2. 2. Rather, a specific component of the cell membrane is concerned in glycerol transfer. 3. 3. This component binds pairs of glycerol molecules to form the penetrating complex. 4. 4. A pair of hydrogen ions or a pair of copper ions are bound to the glycerol binding site and inhibit non-competitively. 5. 5. Structural analogues of glycerol are competitive inhibitors of its transfer. If these inhibitors possess a single hydroxyl group, then a pair of these are required to form the inhibited complex. If the inhibitor possesses two hydroxyl groups, a single molecule of inhibitor can inhibit each glycerol-binding site. 6. 6. These data suggest a mechanism to account for glycerol transfer involving an enzyme-like component of the membrane which catalyses dimer formation between pairs of glycerol molecules to form a complex in which each glycerol molecule acts effectively as a "membrane carrier" for its fellow.

Original languageEnglish
Pages (from-to)47-65
Number of pages19
JournalBiochimica et Biophysica Acta - General Subjects
Volume59
Issue number1
DOIs
StatePublished - 7 May 1962
Externally publishedYes

Fingerprint

Dive into the research topics of 'Spontaneous and enzyme-induced dimer formation and its role in membrane permeability II. The mechanism of movement of glycerol across the human erythrocyte membrane'. Together they form a unique fingerprint.

Cite this