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Stability of erythrocyte ghosts: A γ-ray perturbed angular correlation study

Kruse, Carol A. and Tin, George W. and Baldeschwieler, John D. (1983) Stability of erythrocyte ghosts: A γ-ray perturbed angular correlation study. Proceedings of the National Academy of Sciences of the United States of America, 80 (5). pp. 1212-1216. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:KRUpnas83

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Abstract

The structural integrity of erythrocyte ghosts made by the preswell and slow-dialysis techniques has been studied in vitro by use of γ-ray perturbed angular correlation (PAC) techniques and also by standard in vitro leakage methods employing sequestered labeled markers. Complexes of (111)In(3+) and nitrilotriacetate were encapsulated in ghosts made from human, rabbit, rat, and mouse erythrocytes, and their leakage was monitored by both methods. In addition, (125)I-labeled bovine serum albumin was encapsulated, and ghost integrity was monitored by conventional leakage measurements. With the PAC technique the percentage of material released from human ghosts was determined quantitatively, and the results were equivalent to those obtained by the conventional method. In addition, at various times after intravenous injection, tissue distribution of the ghosts in the mouse was studied. The percent injected dose per gram of tissue of the labeled surface proteins of erythrocyte ghosts in circulation approximated that of the entrapped labeled albumin. This suggests that the ghost membrane and contents are strongly associated in vivo. Large (125)I-labeled bovine serum albumin molecules and small (111)In(3+)-nitrilotriacetate complexes were delivered in high quantities to the lung initially, and to the liver and spleen. Because erythrocyte ghosts have the ability to entrap a wide range of substances and deliver them to specific organs, ghosts may be preferable to other drug carriers or drug therapy for treatment of certain disorders.


Item Type:Article
Additional Information:Copyright © 1983 by the National Academy of Sciences. Contributed by John D. Baldeschwieler, November 29, 1982. This research was supported by grants from the National Institutes of Health (GM-21111-09), the National Science Foundation (CHE-81-12589), and the Monsanto Company. A generous gift from Mr. and Mrs. Lester Finkelstein, Associates of the California Institute of Technology, provided fellowship support for C.A. K. and is gratefully acknowledged. This is contribution no. 6731 from the Arthur Amos Noyes Laboratory of Chemical Physics. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.
Subject Keywords:drug delivery, enzyme replacement, γ-ray probe
Record Number:CaltechAUTHORS:KRUpnas83
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:KRUpnas83
Alternative URL:http://www.pnas.org/cgi/content/abstract/80/5/1212
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:1293
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:09 Jan 2006
Last Modified:14 Nov 2014 19:18

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