PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 415561

Quantitative thyroid fluorescent scanning: technique and clinical experience.

J H Thrall·M T Gillen·M C Johnson·R J Corcoran·L Wartofsky
View original source ↗Export metadata ↓

Abstract

A method for quantifying thyroid gland iodine content using a modified fluorescence scanning system is described. The technique does not require a computer. Two single channel analyzers and digital scalers are used to determine net counts from iodine k-alpha x-rays and system response in counts per milligram is calibrated from studies of known quantities of iodine placed in thyroid phantoms. Fluorescence quantification of thyroid gland iodine content was performed in 250 patients with a wide variety of thyroid disorders. Thirty euthyroid patients judged to have no evidence of thyroid disease averaged 10.1 +/- 3.9 mg glandular iodine. Results for several major diagnostic categories were: untreated Graves' disease, 28 patients, 24.4 +/- 9.9 mg; diffuse euthyroid goiter, 14 patients, 16.1 +/- 7.4 mg; primary hypothyroidism, seven patients, 0.5 mg; and nontoxic multinodular goiter, 28 patients, 7.3 +/- 4.1 mg. Follow-up studies on patients treated for Graves' disease both medically and with 131I generally revealed elevated iodine contents in persistently hyperthyroid patients, lower than normal average amounts in euthyroid patients, and only trace amounts in hypothyroid patients. Although the clinical role of fluorescence iodine quantification remains to be fully established, the technique provides information not otherwise available on an important parameter of thyroid status.

Explore related subjects

FluorescenceGoiterGraves DiseaseHumansHyperthyroidismHypothyroidismIodineMethodsRadionuclide ImagingThyroid DiseasesThyroid GlandJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

J H Thrall, M T Gillen, M C Johnson, R J Corcoran, L Wartofsky. 1978. Quantitative thyroid fluorescent scanning: technique and clinical experience.. https://doi.org/10.2214/ajr.130.3.517

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1992

The chemical synthesis of N-[1-(2-naphthol)]-phosphatidylethanolamine, a fluorescent phospholipid for excited-state proton transfer studies.

A procedure for the preparation of N-[1-(2-naphthol)]-phosphatidylethanolamine (NAPH-PE) has been developed. The synthesis is based on the Schiff base formation between the NH2 of the phospholipid and the aldehyde moiety of 2-hydroxy-1-naphthaldehyde. Then selective reduction of the imine is used to obtain the stable secondary amine, NAPH-PE. Formation of the intermediate Schiff base and the final product is confirmed by 13C- and 1H-NMR. Similar to free 2-naphthol, the excited-state pKa (pKa*) of its phospholipid derivative appears to be significantly lower than the ground-state pKa. At pH 7.4, the excitation spectrum of NAPH-PE shows no deprotonated species in the ground-state, while the emission spectrum presents a significant contribution of this species. Thus the fluorescent phospholipid exhibits the typical behavior of excited-state proton-transfer probes. NAPH-PE is found to incorporate in dimyristoyllecithin (DML) vesicles. The emission spectrum of the probe inserted in the liposomes is affected by acetate used as a proton acceptor. These properties should also be manifest in other lipid bilayers (e.g., plasma membranes of cells) and used for excited-state proton transfer studies.

Fluorescence↗
PubMed1992

Plasma protein binding of quinine: binding to human serum albumin, alpha 1-acid glycoprotein and plasma from patients with malaria.

The binding of quinine to human serum albumin (HSA), alpha 1-acid glycoprotein (AAG) and plasma obtained from healthy subjects (10 caucasians and 15 Thais) and from Thai patients with falciparum malaria (n = 20) has been investigated. In healthy volunteers, plasma protein binding expressed as the percentage of unbound quinine was 7.9-31.0% (69-92.1% bound). The mean percentage of unbound quinine found with essentially fatty acid-free HSA (40 g L-1) was 65.4 +/- 1.5% (mean +/- s.d.) and was comparable with the value (66.3 +/- 3.8%, mean +/- s.d.) for Fraction V HSA (40 g L-1). This suggests that fatty acids do not influence the plasma protein binding of quinine. Binding of quinine to 0.7 g L-1 AAG was high (mean unbound 61.0 +/- 5.0%), indicating that quinine is bound primarily to AAG and albumin, although other plasma proteins such as lipoproteins may be involved. The mean percentage of unbound quinine was slightly less in caucasians (14.8 +/- 6.7% unbound), compared with healthy Thai subjects (17.0 +/- 6.7% unbound). The higher binding of quinine in caucasian subjects was associated with a higher plasma AAG concentration observed in caucasians. Mean percentage of unbound quinine was significantly lower in Thai patients with malaria (10.9 +/- 4.0%) than in the healthy Thai subjects. The increase in the extent of quinine binding corresponded with the increase in the acute-phase reactant protein, AAG in the patients with malaria. Overall, when the data were combined there was a significant correlation (r = 0.846, P < 0.005) between the binding ratio (bound/unbound) of quinine and the plasma AAG concentration.(ABSTRACT TRUNCATED AT 250 WORDS)

Fluorescence↗
PubMed1992

Subunit interactions of vesicular stomatitis virus envelope glycoprotein stabilized by binding to viral matrix protein.

The mechanism by which viral glycoproteins are incorporated into virus envelopes during budding from host membranes is a major question of virus assembly. Evidence is presented here that the envelope glycoprotein (G protein) of vesicular stomatitis virus binds to the viral matrix protein (M protein) in vitro with the specificity, reversibility, and affinity necessary to account for virus assembly in vivo. The assay for the interaction is based on the ability of M protein to stabilize the interaction of G protein subunits, which exist as trimers of identical subunits in the virus envelope. The interaction with M protein was shown by using G proteins labeled with fluorescent probes capable of detecting subunit dissociation and reassociation in vitro. The results show that the M protein isolated from virions either as purified soluble protein or as nucleocapsid-M protein complexes interacts with the G protein in vitro and that the reaction is reversible. The interaction between the G and M proteins was not serotype specific, but no interaction between the vesicular stomatitis virus M protein and the influenza virus hemagglutinin could be detected. These results support the conclusion that the interactions described here are the ones that govern assembly of G protein into virus envelopes in vivo.

Fluorescence↗