JNM
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

The Journal of Nuclear Medicine Vol. 29 No. 1 62-67
© 1988 by Society of Nuclear Medicine
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zanelli, G. D.
Right arrow Articles by Woolley, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zanelli, G. D.
Right arrow Articles by Woolley, G.

Protein Binding Studies of Technetium-99m-Labeled Phosphine and Isocyanide Cationic Complexes

Giuseppe D. Zanelli, Neil Cook, Avijit Lahiri, David Ellison, Peter Webbon and Gillian Woolley

Divisions of Radioisotopes and Clinical Sciences, Clinical Research Centre, Northwick Park Hospital, Harrow, Middlesex
Department of Cardiology, Northwick Park Hospital, Harrow, Middlesex
Royal Veterinary School, North Mymms, Herts, UK

Correspondence: For reprints contact: G.D. Zanelli, MD, Radioisotopes Division, Clinical Research Centre, Watford Rd., Harrow, Middlesex HA1 3UJ, United Kingdom.

ABSTRACT

Most 99mTc/phosphine/isocyanide complexes synthesized to date show preferential uptake by the myocardium of many animal species but not in man. A new complex has been synthesized, [99mTc(DEPE)2(CNR)2],+(DEPIC), where R = t — butyl isocyanide, which in three animal species images the myocardium very well, but in humans it remains primarily in the blood pool. One reason for the difference in the behavior of these complexes in different species could be the characteristics of their binding to plasma proteins. The protein binding characteristics of DEPIC and two other well-known complexes have therefore been studied. Whereas the other complexes bind nonspecifically to many proteins both in animal and human plasma, DEPIC binds almost exclusively to prealbumin in humans but nonspecifically to other proteins in the rabbit. The binding sites in human plasma appear to be those normally occupied by thyroxine on the prealbumin tetramer and these can be blocked by sodium salicylate.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
JOURNAL OF NUCLEAR MEDICINE TECHNOLOGY THE JOURNAL OF NUCLEAR MEDICINE
Copyright © 1988 by the Society of Nuclear Medicine.