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M W Simpson-Morgan

Publications and source records attributed to M W Simpson-Morgan.

30 records · Page 2Linked to original sources
PubMed1976

The transcapillary exchange of thyroid hormones and thyroxine-binding proteins between blood and tissue fluids.

A study has been made of the relative importance of potien bound and unbound hormone in the exchange of thyroid hormones between blood and interstitial fluid. 2. When [I] tyroxine (or thriiodothyronine) and [I] human serum albumin were injected simultaneously into the circulation of sheep with chronic lymphatic fistulae, the thyroid hormones were removed from the circulation and apperaed in all lymph samples at a greater fractional rate than human serum albumin. 3. The steady-state lymph/plasma concentrations ratios of the two specific thyroxine binding proteins were similar to each other and to those of albmin and total thyroxine. 4. Gel filtration studies indicated that the two specific thyroxine binding proteins, ovine serum albumin and human serum albumin, were all of similar molecular size. 5. Concentrations of unbound thyroxine in plasma and various samples of lymph from the one animal were similar. 6. Increasing the proportion of thyroid hormone that was unbound resulted in an increase rate of equilibration of labelled hormone between blood plasma and lymph. 7. Perfusion of the popliteal lymph node demonstrated that thyroid hormones were removed from lymph during its passage through the node. The amount removed was related to the proportion of hormone in the unbound state.

Animals↗
PubMed1975

The thyroxine-binding properties of serum proteins. A competitive binding technique employing sephadex G-25.

A competitive binding technique is described for the estimation of the thyroxine (T4)-binding properties of serum proteins in dilute blood serum and lymph. When used in conjunction with an assay for total T4 the following parameters can be estimated: the number of functionally different T4 binding proteins, their individual association constants and binding capacities for T4, the amount of T4 which is bound to each binding species, and the concentration of unbound (free) T4. Both human and sheep serum have three functionally different T4-binding proteins. The association constants for the three human proteins were 9.5x10(9), 1.6x10(8) and 3.1x10(5) 1/mol for T4-binding globulin (TBG), T4-binding prealbumin (TBPA) and serum albumin, respectively. The corresponding sheep proteins, TBG, TBP-2 and albumin, had association constants of 8.9x10(9), 1-4 X 10(8) and 3.5x10(5) 1/mol. Human TBG had a mean binding capacity of 21.3 mug/100 ml and that of ovie TBG was 12.8 mug/100 ml. The other specific binding proteins (TBPA in man and TBP-2 in sheep) had mean binding capacities of 307 and 359 mug/100 ml respectively. Two functionally different T4-binding proteins were identified in rat serum.

Animals↗
PubMed1975

Effect of ionic strength and ionic composition of assay buffers on the interaction of thyroxine with plasma proteins.

When plasma proteins are diluted with buffer the ionic strength and ionic composition of that buffer affects the interactions between thyroxine (T4) and its plasma protein-binding sites. Increases in phosphate, chloride or barbiturate ion concentration from 50 to 200 mmol/l caused a significant decrease in the affinity of plasma proteins for T4, and a concurrent increase in the concentration of unbound T4. These results cannot be completely accounted for by changes in ionic strength since at the same ionic strength different anions caused quantitatively different effects on unbound T4 concentration. The degree of depression of T4 binding by the three anions studied was in the order barbiturate greater than chloride greater than phosphate. The results of a systematic study on the composition of diluent buffer systems indicated that when a 50 mM-sodium phosphate-100 mM-NaCl buffer (pH 7-4) was used as a plasma diluent, there were unlikely to be gross changes in the T4-binding properties of plasma proteins with dilution.

Barbiturates↗
PubMed1974

Relative rates of transcapillary movement of free thyroxine, protein-bound thyroxine, thyroxine-binding proteins, and albumin.

The rate of appearance of labeled thyroxine (T4) and albumin in lymph from various areas after simultaneous i.v. injection of the labeled substances in conscious ambulatory sheep has been used to estimate the relative rates of transcapillary movement of stable T4 and albumin. Labeled T4 appeared in hepatic lymph at the same rate as albumin. In intestinal and leg lymph, labeled T4 appeared eight and four times as rapidly as albumin indicating that T4 crosses capillaries in these areas independently of and much more rapidly than albumin and other proteins having similar distribution kinetics. The lymph:plasma ratios for all the T4-binding proteins including albumin were very similar in any one area showing that the relative fractional rates of transcapillary movement of these proteins were very similar. Therefore in extrahepatic areas, transcapillary movement of T4 in the protein-bound form was quantitatively much less important than in the free form. The findings support earlier views, recently questioned, that free T4 is of considerable physiological significance.

Animals↗
PubMed1968

The metabolism of chylomicron fatty acids by isolated rat heart-lung preparations.

1. An isolated rat heart-lung preparation is described. This preparation is perfused with the rat's own blood, in the absence of heparin or other anticoagulants, by the sustained efficient contractions of the heart. The preparation has only a small circulating blood volume and is stable for up to 3 hr.2. Chylomicrons which were infused continuously into the circulating blood of the heart-lung preparation were removed from the circulation.3. [(14)C]Palmitic acid incorporated into the chylomicrons was oxidized rapidly to CO(2). Rates of oxidation of chylomicron fatty acids in excess of 3 mg/hr were measured and suggest that in the intact rat, the heart and lungs could account for up to 10% of the chylomicron fatty acids oxidized.4. The infusion of glucose did not reduce the oxidation of the chylomicron fatty acids, whilst the infusion of sufficient quantities of chylomicrons in the absence of glucose spared some of the cardiac glycogen.

Animals↗