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Biomedical subjects

E I McDougall

Publications and source records attributed to E I McDougall.

11 recordsLinked to original sources
PubMed1985

Multiple sclerosis in research workers studying swayback in lambs: an updated report.

Four out of seven research workers into swayback disease, a neurological disease of lambs, developed symptoms and signs of multiple sclerosis, and were reported in 1947. A further worker later joined the group. All of the original seven have died and two at necropsy had multiple areas of demyelination in the brain and spinal cord. The chance of four or more out of a random group of eight men developing multiple sclerosis is about one in a thousand million. Multiple sclerosis has not occurred in other workers on swayback disease elsewhere.

Adult↗
PubMed1977

The state of aggregation of red deer (Cervus elaphus L.) beta-lactoglobulin preparations near neutral pH.

1. The state of aggregation of four red-deer (Cervus elaphus L.) beta-lactoglobulin preparations and a control ox beta-lactoglobulin A preparation was studied by sedimentation-equilibrium experiments at pH 6.5 and 20 degrees C. 2. Three of the deer preparations and the ox control each behaved as a monomer-dimer system, with a value of log K (where K is the association constant in litres/mol) in the range 5.4-5.5. 3. When one of these deer preparations was examined in the presence of dithiothreitol, log K appeared to decrease to 4.5.4. One deer preparation, comprising recovered material, appeared to have undergone irreversible changes and to behave like a non-equilibrating system containing monomer, dimer and trimer. 5. The sedimentation-equilibrium properties of the deer monomer was studied in 6M-guanidine hydrochloride at pH 7.0; the mol.wt. was 17600, the second virial coefficient was 3.4 x 10(-3) ml - mol - g-2, and the apparent partial specific volume 0.724 ml/g, a value indicating an appreciable decrease in volume on dissociation and denaturation.

Animals↗
PubMed1976

The whey proteins of the milk of red deer (Cervus elaphus L.). A homologue of bovine beta-lactoglobulin.

1. The whey proteins from the milk of red deer are compared with those of cattle. Gel chromatography and electrophoresis showed a close similarity between the whey proteins of the two species in the size, mobility and relative amounts of the main constituents and in the changes in their relative amounts with time after parturition. 2. The major constituent of the deer whey was isolated. It appeared to be homologous with bovine beta-lactoglobulin and had the following properties: m=-5.2X10(-9)m2-s-1-V-1 at 4 degrees C and pH 8.6; pI=5.17; S020, w =2.89S; v=0.748 ml/g; E1g/dl 1cm= 9.12 at 278 nm; deltan/c=1.794 X 10(-3)dl/g at 579 nm (all at 20 degrees C except m). Its molecular weight was that of a dimer with a subunit weight of 18 000. 3. Amino acid analyses of this protein, adjusted to lysine = 15 residues showed that it contains one more residue of aspartic acid, alanine and methionine and one less glutamic acid residue and two less leucine residues than bovine beta-lactoglobulin A. 4. On starch-gel electrophoresis at pH 8.2, this protein migrated at the same rate as bovine beta-lactoglobulin B, although its isoelectric point is close to that of the bovine A variant. Milk from three out of 27 hinds examined showed a variant. This migrated in starch gel at the same rate as the bovine A variant but had a more acid pI = 5.02. 5. The two species whose milk whey proteins are compared represent two different families of ruminants. The similarities found support the view that the milk whey proteins of the bovids are probably typical of the suborder as a whole.

Amino Acids↗
PubMed1966

Proteins of the succus entericus from the jejunum of the sheep.

1. Suitable methods for studying the proteins passing into the small intestine are discussed. 2. The proteins passing into temporarily isolated jejunal loops between double re-entrant fistulae in four sheep were studied. 3. Loops about 60-70cm. long secreted protein at a rate of 1-5g./24hr. The effect of slight stimulation of secretion by air pressure on the output of protein in 24hr. was not regular. The total protein in the fluid part of the succus entericus is about 2(1/2) times the serum albumin content of the fluid. 4. The additional protein contained in the cellular debris amounts to about 60% of the protein in the fluid part of the succus entericus. 5. Comparison of the proteins in succus entericus with those in serum by immunoelectrophoretic and other electrophoretic methods showed eight components in the fluid part of the succus entericus that appeared to be the same as those in serum and two components that appeared not to be present in serum. 6. Thin-layer gel chromatography in Sephadex G-200 and sedimentation analysis showed that the succus entericus contained two proteins not present in serum, one with sedimentation coefficient (uncorrected) 10s and one sedimenting slower than albumin: they move with the macroglobulin and slower than albumin respectively on gel chromatography. 7. These proteins could be secreted by the glandular epithelium of the small intestine or liberated from desquamated epithelial cells.

Animals↗