Spectrophotometric determination of monoiodotyrosine, diiodotyrosine, and thyroxine in iodoproteins

Covelli, I; Zyl, A. Van; Edelhoch, Harold

doi:10.1016/0003-2697(71)90012-1

Cited by 23 publications

(4 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The fraction containing TG was again dialyzed and lyophilized. This preparation was shown to be homogeneous by sucrose density gradient ultracentrifugation and without thyroxine by the spectrophotometric titration method of Covelli et al [9]. Antibody to thyroxine-free human TG was produced in rabbits.…”

Section: Methodsmentioning

confidence: 99%

Effects of TSH stimulation on serum thyroglobulin in metastatic thyroid cancer

Gerfo

Colacchio

et al. 1980

Journal of Surgical Oncology

View full text Add to dashboard Cite

Thyroglobulin (TG) is a glycoprotein which has been found to be produced by almost all nonmedullary thyroid cancers, and is present in elevated levels in the serum of most patients with metastatic thyroid cancer. It has long been a clinical impression that many metastatic thyroid cancers are "responsive" to TSH suppression as manifested by a decrease in the size and/or symptoms of the tumor. Five athyroid patients with metastatic thyroid cancer were studied to determine the effect of TSH stimulation on their serum TG levels and attempt to correlate this effect with their clinical response. Three of the five patients showed a definite rise in their serum TG once serum thyroxine (T4Y replacement was withdrawn, which correlated with an increase in TSH, and two of these patients have had no progression of their disease while on T4 suppression. The remaining two patients have shown no change in their TG levels after T4 withdrawal, and both have had progression of their metastatic disease while on T4 suppression. Thus, we see that in some patients, TG production by their metastatic thyroid cancer is responsive to TSH suppression, and there is some suggestion that TSH-responsive cancers are less aggressive; but it will require further studies to determine this.

show abstract

Section: Methodsmentioning

confidence: 99%

Effects of TSH stimulation on serum thyroglobulin in metastatic thyroid cancer

Gerfo

Colacchio

et al. 1980

Journal of Surgical Oncology

View full text Add to dashboard Cite

show abstract

“…The run was carried out using 6O/, cyanogum-41 as gel in a jacketed column maintained a t 4 "C. The buffer was 0.05 M Tris-C1 pH 9.9 a t the start of the run. Spectrophotometric analyses of the iodinated protein were performed in 8 M urea as described elsewhere [15,16].…”

Section: Protein Determinationsmentioning

confidence: 99%

“…-, Absorbance a t 278 nm; ----, radioactivity The level of iodination in the protein peaks was determined by spectrophotometric analysis of the constituent the iodioamino acids [15,16]. The pertentage distribution of iodoamino acids in the pooled tubes from each electrophoretic peak is listed in Table 1.…”

Section: Preparation Of the Labeled Monoiodotyrosylmentioning

confidence: 99%

Synthesis of Bioactive 131I-Labeled Epidermal Growth Factor and Its Distribution in Rat Tissues

et al. 1972

View full text Add to dashboard Cite

Radioactive monoiodotyrosyl epidermal growth factor has been synthesized and purified by means of preparative gel electrophoresis. The labeled product retains full biological activity, as compared to that of the native epidermal growth factor. In more extensively iodinated derivatives the biological activity decreases as a function of the degree of iodination. The purified 131I‐labeled epidermal growth factor has been injected intraperitoneally in the rat and its distribution in some peripheral tissues such as liver, spleen, cornea, lung, heart, epidermis, skeletal muscle, kidney, brain, pancreas, intestine and testis, followed as a function of time. Only two tissues concentrate 131I‐labeled epidermal growth factor with respect to the blood: the epidermis (about + 300%) and the epithelial cells of the cornea (about + 800%). The addition in vitro of native epidermal growth factor is able either to inhibit the binding of the labeled growth factor to the target tissues, or to discharge it after binding in a way which suggests a competition for the specific receptor sites.

show abstract

“…The thyroglobulin 19 S molecule is only apparently homogeneous (Ingbar et al 1959;Ui et al 1961;Robbins 1963;Robbins et al 1966;Salvatore 8c Edelhoch 1973); a number of investigators have shown the heterogeneity of 19 S thyro¬ globulin with regard to its iodine composition (Edelhoch 1962;Van Zyl 8c Edelhoch 1967;de Crombrugghe et al 1967;Edelhoch 8c Perlman 1968;Taurog 1970Taurog , 1974Rolland et al 1970Rolland et al , 1972Covelli et al 1971;Lamas 8c Morreóle de Escobar 1972;Sorimachi 8c Ui 1974è;Tarutani et al 1975). Using an ion exchange Chromatographie method to purify thyroglobulin, various subfractions with different iodine contents have been isolated (Ui et al 1961;Robbins 1963;Robbins et al 1966;Sorimachi 8c Ui 1974«).…”

mentioning

confidence: 99%

Iodoamino Acid Composition of Poorly Iodinated Human Thyroglobulin Fractionated by Isopycnic Centrifugation

Vignal

Nataf

Tubiana

1978

Acta Endocrinologica

View full text Add to dashboard Cite

The distribution of iodotyrosines and iodothyronines has been studied in poorly iodinated 19 S thyroglobulins isolated by sucrose gradient centrifugation from five human thyroid tissue. The 19 S thyroglobulins have been fractionated by isopycnic centrifugation in 34.5 % rubidium chloride gradient. The distribution of iodoamino acids depends on the total iodine content of each fraction. The variations in MIT1) and DIT residues with

show abstract

Spectrophotometric determination of monoiodotyrosine, diiodotyrosine, and thyroxine in iodoproteins

Cited by 23 publications

References 7 publications

Effects of TSH stimulation on serum thyroglobulin in metastatic thyroid cancer

Effects of TSH stimulation on serum thyroglobulin in metastatic thyroid cancer

Synthesis of Bioactive 131I-Labeled Epidermal Growth Factor and Its Distribution in Rat Tissues

Iodoamino Acid Composition of Poorly Iodinated Human Thyroglobulin Fractionated by Isopycnic Centrifugation

Contact Info

Product

Resources

About