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Journal Articles

Kinetics of bicarbonate transport in human red blood cell membranes at body temperature.

P K Gasbjerg, P A Knauf, J Brahm

J Gen Physiol (1996) 108 (6): 565–575.

https://doi.org/10.1085/jgp.108.6.565

Published: 01 December 1996

View articletitled, Kinetics of bicarbonate transport in human red blood cell membranes at body temperature.

Journal Articles

The asymmetry of chloride transport at 38 degrees C in human red blood cell membranes.

P A Knauf, P K Gasbjerg, J Brahm

J Gen Physiol (1996) 108 (6): 577–589.

https://doi.org/10.1085/jgp.108.6.577

Published: 01 December 1996

View articletitled, The asymmetry of chloride transport at 38 degrees C in human red blood cell membranes.

Journal Articles

Effects of external pH on substrate binding and on the inward chloride translocation rate constant of band 3.

S Q Liu, F Y Law, P A Knauf

J Gen Physiol (1996) 107 (2): 271–291.

https://doi.org/10.1085/jgp.107.2.271

Published: 01 February 1996

View articletitled, Effects of external pH on substrate binding and on the inward chloride translocation rate constant of band 3.

Journal Articles

Effects of external pH on binding of external sulfate, 4.4-dinitro-stilbene-2,2'-disulfonate (DNDS), and chloride to the band 3 anion exchange protein.

S Q Liu, E Ries, P A Knauf

J Gen Physiol (1996) 107 (2): 293–306.

https://doi.org/10.1085/jgp.107.2.293

Published: 01 February 1996

View articletitled, Effects of external pH on binding of external sulfate, 4.4-dinitro-stilbene-2,2'-disulfonate (DNDS), and chloride to the band 3 anion exchange protein.

Journal Articles

A novel method to differentiate between ping-pong and simultaneous exchange kinetics and its application to the anion exchanger of the HL60 cell.

D Restrepo, B L Cronise, R B Snyder, P A Knauf

J Gen Physiol (1992) 100 (5): 825–846.

https://doi.org/10.1085/jgp.100.5.825

Published: 01 November 1992

View articletitled, A novel method to differentiate between ping-pong and simultaneous exchange kinetics and its application to the anion exchanger of the HL60 cell.

Journal Articles

pH homeostasis in promyelocytic leukemic HL60 cells.

D Restrepo, D J Kozody, L J Spinelli, P A Knauf

J Gen Physiol (1988) 92 (4): 489–507.

https://doi.org/10.1085/jgp.92.4.489

Published: 01 October 1988

View articletitled, pH homeostasis in promyelocytic leukemic HL60 cells.

Journal Articles

Mechanism of the increase in cation permeability of human erythrocytes in low-chloride media. Involvement of the anion transport protein capnophorin.

G S Jones, P A Knauf

J Gen Physiol (1985) 86 (5): 721–738.

https://doi.org/10.1085/jgp.86.5.721

Published: 01 November 1985

View articletitled, Mechanism of the increase in cation permeability of human erythrocytes in low-chloride media. Involvement of the anion transport protein capnophorin.

Journal Articles

Transmembrane effects of intracellular chloride on the inhibitory potency of extracellular H2DIDS. Evidence for two conformations of the transport site of the human erythrocyte anion exchange protein.

W Furuya, T Tarshis, F Y Law, P A Knauf

J Gen Physiol (1984) 83 (5): 657–681.

https://doi.org/10.1085/jgp.83.5.657

Published: 01 May 1984

View articletitled, Transmembrane effects of intracellular chloride on the inhibitory potency of extracellular H2DIDS. Evidence for two conformations of the transport site of the human erythrocyte anion exchange protein.

Journal Articles

Use of niflumic acid to determine the nature of the asymmetry of the human erythrocyte anion exchange system.

P A Knauf, N A Mann

J Gen Physiol (1984) 83 (5): 703–725.

https://doi.org/10.1085/jgp.83.5.703

Published: 01 May 1984

View articletitled, Use of niflumic acid to determine the nature of the asymmetry of the human erythrocyte anion exchange system.

Journal Articles

Effects of the transport site conformation on the binding of external NAP-taurine to the human erythrocyte anion exchange system. Evidence for intrinsic asymmetry.

P A Knauf, F Y Law, T Tarshis, W Furuya

J Gen Physiol (1984) 83 (5): 683–701.

https://doi.org/10.1085/jgp.83.5.683

Published: 01 May 1984

View articletitled, Effects of the transport site conformation on the binding of external NAP-taurine to the human erythrocyte anion exchange system. Evidence for intrinsic asymmetry.

Journal Articles

Relationship of net chloride flow across the human erythrocyte membrane to the anion exchange mechanism.

P A Knauf, F Y Law, P J Marchant

J Gen Physiol (1983) 81 (1): 95–126.

https://doi.org/10.1085/jgp.81.1.95

Published: 01 January 1983

View articletitled, Relationship of net chloride flow across the human erythrocyte membrane to the anion exchange mechanism.

Journal Articles

N-(4-azido-2-nitrophenyl)-2-aminoethylsulfonate (NAP-taurine) as a photoaffinity probe for identifying membrane components containing the modifier site of the human red blood cell anion exchange system.

P A Knauf, W Breuer, L McCulloch, A Rothstein

J Gen Physiol (1978) 72 (5): 631–649.

https://doi.org/10.1085/jgp.72.5.631

Published: 01 November 1978

View articletitled, N-(4-azido-2-nitrophenyl)-2-aminoethylsulfonate (NAP-taurine) as a photoaffinity probe for identifying membrane components containing the modifier site of the human red blood cell anion exchange system.

Journal Articles

Asymmetry of the red cell anion exchange system. Different mechanisms of reversible inhibition by N-(4-azido-2-nitrophenyl)-2-aminoethylsulfonate (NAP-taurine) at the inside and outside of the membrane.

P A Knauf, S Ship, W Breuer, L McCulloch, A Rothstein

J Gen Physiol (1978) 72 (5): 607–630.

https://doi.org/10.1085/jgp.72.5.607

Published: 01 November 1978

View articletitled, Asymmetry of the red cell anion exchange system. Different mechanisms of reversible inhibition by N-(4-azido-2-nitrophenyl)-2-aminoethylsulfonate (NAP-taurine) at the inside and outside of the membrane.

Journal Articles

The relationship between anion exchange and net anion flow across the human red blood cell membrane.

P A Knauf, G F Fuhrmann, S Rothstein, A Rothstein

J Gen Physiol (1977) 69 (3): 363–386.

https://doi.org/10.1085/jgp.69.3.363

Published: 01 March 1977

View articletitled, The relationship between anion exchange and net anion flow across the human red blood cell membrane.

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Kinetics of bicarbonate transport in human red blood cell membranes at body temperature.

The asymmetry of chloride transport at 38 degrees C in human red blood cell membranes.

Effects of external pH on substrate binding and on the inward chloride translocation rate constant of band 3.

Effects of external pH on binding of external sulfate, 4.4-dinitro-stilbene-2,2'-disulfonate (DNDS), and chloride to the band 3 anion exchange protein.

A novel method to differentiate between ping-pong and simultaneous exchange kinetics and its application to the anion exchanger of the HL60 cell.

pH homeostasis in promyelocytic leukemic HL60 cells.

Mechanism of the increase in cation permeability of human erythrocytes in low-chloride media. Involvement of the anion transport protein capnophorin.

Transmembrane effects of intracellular chloride on the inhibitory potency of extracellular H2DIDS. Evidence for two conformations of the transport site of the human erythrocyte anion exchange protein.

Use of niflumic acid to determine the nature of the asymmetry of the human erythrocyte anion exchange system.

Effects of the transport site conformation on the binding of external NAP-taurine to the human erythrocyte anion exchange system. Evidence for intrinsic asymmetry.

Relationship of net chloride flow across the human erythrocyte membrane to the anion exchange mechanism.

N-(4-azido-2-nitrophenyl)-2-aminoethylsulfonate (NAP-taurine) as a photoaffinity probe for identifying membrane components containing the modifier site of the human red blood cell anion exchange system.

Asymmetry of the red cell anion exchange system. Different mechanisms of reversible inhibition by N-(4-azido-2-nitrophenyl)-2-aminoethylsulfonate (NAP-taurine) at the inside and outside of the membrane.

The relationship between anion exchange and net anion flow across the human red blood cell membrane.

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