The nature of the membrane sites controlling anion permeability of human red blood cells as determined by studies with disulfonic stilbene derivatives.

The Journal of membrane biology ·Vol. 10 ·No. 3 ·1972-12-29 ·Pages 311-30

Cabantchik ZI, Rothstein A

Abstract

暂无摘要

MeSH Terms

Binding Sites Biological Transport/drug effects Blood Proteins Carbon Radioisotopes Cell Membrane Permeability Chlorides/metabolism Electrophoresis, Polyacrylamide Gel Erythrocytes/cytology,drug effects,metabolism Humans Iodine Radioisotopes Kinetics Molecular Weight Protein Binding Radioisotopes Spectrometry, Fluorescence Stilbenes/chemical synthesis,pharmacology Structure-Activity Relationship Sulfates/metabolism Sulfonic Acids/chemical synthesis,pharmacology Sulfur Radioisotopes

Chemicals

Blood Proteins Carbon Radioisotopes Chlorides Iodine Radioisotopes Radioisotopes Stilbenes Sulfates Sulfonic Acids Sulfur Radioisotopes

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Cabantchik Z I

Rothstein A

References (20)

20 references, click to expand

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Article Info

Journal

The Journal of membrane biology

Abbr.

J Membr Biol

ISSN

0022-2631

DOI

10.1007/BF01867863

Published

1972-12-29

Pages

311-30

Language

English

Region

United States

NLM ID

0211301

Subset

External Links

PubMed source DOI: 10.1007/BF01867863 View journal details

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The nature of the membrane sites controlling anion permeability of human red blood cells as determined by studies with disulfonic stilbene derivatives.

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