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Biomedical subjects

E H Morgan

Publications and source records attributed to E H Morgan.

At least 145 records · Page 8Linked to original sources
PubMed1976

A test of the practical value of estimating breath sound intensity. Breath sounds related to measured ventilatory function.

Each of four examiners performed standardized physical examinations on a group of patients who had just undergone tests of ventilatory function. The intensity of breath sounds heard with deep inspiration was graded on a rating scale of 0 to 4; the grades in six areas of the chest were added to give a total score, with possible values ranging from 0 to 24. Correlation of breath-sound scores with percentage of predicted forced expiratory volume in one second (FEV1) was significant at the 1 percent level for all of the examiners. Differences between the examiners in their assessment of breath sounds were not statistically significant. Grading the loudness of breath sounds was a poor screening test for mild ventilatory abnormality, but normal breath sounds nearly excluded the possibility of severe reduction in the FEV1. Definitely reduced breath-sound intensity was strong evidence for the presence of obstructive pulmonary disease.

Adult↗
PubMed1975

Mossbauer spectra of bicarbonate-free ferric-transferrin complex.

The bicarbonate-free ferric-transferrin complex was investigated by Mossbauer Spectroscopy under anaerobic conditions. No evidence of specific binding was found. The spectral results indicates that the apparent binding is due to the formation of antiferromagnetic ferric hydroxide polymers which are firmly attached to the transferrin molecule. Specific binding would only occur in the presence of bicarbonate or other low molecular weight chelators.

Animals↗
PubMed1975

Factors affecting incorporation of (14C) leucine into albumin and transferrin by the liver in the postnatal rat.

The mechanisms responsible for the increase in incorporation of radioactive amino acid into albumin, transferrin and total soluble liver protein which occurs in the immediate postnatal period in the rat was investigated in rats delivered surgically in the last 2 days of gestation. The in vivo incorporation of [14C]leucine into the proteins in the liver was low at birth, but increased rapidly during the first half hour after delivery and then more gradually during the subsequent 4.5 h. Neonatal adrenalectomy had no effect on this pattern of results. Intraperitoneal administration of an amino acid supplement had little effect on [14C]leucine incorporation immediately after birth but increased incorporation at 0.5 h and eliminated the second phase of rising incorporation values between 0.5 and 5 h. The in vitro incorporation of 14C into albumin, transferrin and total protein by slices of the liver from animals immediately after delivery was as great as with slices from animals 5 h after delivery. It is concluded that the initial increase in synthesis of proteins in the liver in the first 0.5 h after delivery is probably due to an increase in the supply of metabolic energy due to improved oxygenation of the rats and that the slower increase in protein synthesis between 0.5-5.0 h results from an improved supply of amino acids to liver cells. It is unlikely that changes in the secretion of adrenal hormones in involved.

Adrenal Glands↗
PubMed1975

Plasma iron transport during egg laying and after oestrogen administration in the domestic fowl (Gallus domesticus).

The concentrations of 59Fe and of radioiodinated transferrin and albumin were measured in the blood, liver, spleen, bone marrow and ova at different times after the injection of transferrin-bound 59Fe and the labelled proteins into non-laying, laying and oestrogen treated chickens. In the egg-laying and oestrogen-treated birds the 59Fe of the plasma was rapidly transferred from transferrin to another component with the properties of th phosphoprotein, phosvitin. Radioactive iron, and labelled transferrin and albumin to a lesser extent, entered the ova only while they were in the ovary. Relatively more labelled transferrin than albumin was found in all the tissues studied except in the ova, in which the two labelled proteins were present in the same relative concentration as in the plasma. It is concluded that, during egg laying and after oestrogen treatment, plasma iron bound to transferrin is taken up by the liver, incorporated into phosvitin and is then secreted into the plasma leading to elevation of the plasma iron concentration and transfer of iron to the ova.

Animals↗
PubMed1974

Albumin and transferrin synthesis during development in the rat.

In this study, the incorporation of [(14)C]leucine into albumin and transferrin in early rat foetuses, vitelline plus amniotic membranes, chorioallantoic placenta and perinatal rat liver slices was measured and used to detect and compare the rates of synthesis of the two proteins. Albumin synthesis was detected in the body of foetuses from 13 days gestation onwards. Transferrin synthesis was detected only after day 15. Transferrin synthesis was demonstrable in the membranes but not in the chorioallantoic placenta of all the animals investigated, i.e. from 13 to 19 days gestation. Synthesis of albumin and transferrin by the liver of near-term and postnatal animals was shown to correlate with published data on the parenchymal cell number/unit wet wt. of liver. Near-term foetuses synthesized relatively more transferrin than albumin when compared with 10-day postnatal animals. The serum concentrations of the two plasma proteins were also determined. These increased before term whereas the rate of synthesis of albumin and transferrin declined. Postnatally, plasma albumin concentration increased but transferrin concentration decreased, yet the rates of synthesis of both proteins by the liver increased with age. This lack of correlation between the rates of synthesis of the two proteins and their respective plasma concentrations could be explained in part by their increased stability after birth. There was also evidence that the liver haemopoietic cells took up transferrin although they do not synthesize the protein. Thus the decrease in this population of cells during development could also contribute to the discrepancy between liver synthesis and serum concentrations of transferrin.

Age Factors↗