TY - JOUR
T1 - Spontaneous and enzyme-induced dimer formation and its role in membrane permeability II. The mechanism of movement of glycerol across the human erythrocyte membrane
AU - Stein, W. D.
PY - 1962/5/7
Y1 - 1962/5/7
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0008736738&partnerID=8YFLogxK
U2 - 10.1016/0006-3002(62)90697-2
DO - 10.1016/0006-3002(62)90697-2
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C2 - 13916652
AN - SCOPUS:0008736738
SN - 0006-3002
VL - 59
SP - 47
EP - 65
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
IS - 1
ER -