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Biomedical subjects

J L Woods

Publications and source records attributed to J L Woods.

9 recordsLinked to original sources
PubMed1994

Immobilised pH gradient isoelectric focusing of wool proteins.

Conventional carrier ampholyte-isoelectric focusing is unsuitable for separating wool and hair proteins. The inability to form stable narrow pH gradients at acidic pH values does not allow good resolution of the many acidic wool and hair proteins. To evaluate the usefulness of immobilised pH gradient-isoelectric focusing (IPG-IEF) for wool proteins, S-amidomethyl wool proteins were analysed using IPG-IEF. Over twenty bands were visible on a pH 4-7 IPG-IEF gel. IPG-IEF was combined with sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) to give a two dimensional separation, and over 50 protein spots were observed. IPG-IEF appears to be ideally suited to the separation of wool proteins. The resolution of two-dimensional electrophoresis using IPG-IEF was greater than previously obtained using acid or alkaline PAGE in the first dimension. Good reproducibility of spot position was observed.

Ampholyte Mixtures↗
PubMed1991

Chimeric antithrombin peptide. Characterization of an Arg-Gly-Asp (RGD)- and hirudin carboxyl terminus-containing synthetic peptides.

We investigated the properties of an artificial chimeric peptide that contains an Arg-Gly-Asp (RGD)-tripeptide, the versatile cell recognition signal of extracellular matrix protein components, coupled to a carboxyl-terminal fragment of the highly specific alpha-thrombin inhibitor, hirudin (residues 53-64): WGRGDSANGDFEEIPEEYL (RGD-hirudin53-64). Hirudin53-64 and RGD-hirudin53-64 inhibited the fibrinogen clotting activity of alpha-thrombin and prolonged the activated partial thromboplastin time of human plasma. In addition, both peptides afforded total protection to thrombin from trypsionolysis. Neither hirudin53-64 nor RGD-hirudin53-64 dramatically interfered with the thrombin-antithrombin inhibition reaction either in the absence or presence of added heparin. alpha-Thrombin-induced platelet aggregation was effectively inhibited by hirudin53-64 and RGD-hirudin53-64. Unlike hirudin53-64, RGD-hirudin53-64 in solution inhibited integrin-mediated endothelial cell and fibroblast cell attachment to polystyrene wells in the presence of fetal bovine serum. Collectively, our results demonstrate that RGD-hirudin53-64 has anticoagulant/antiplatelet aggregation activity attributable to its hirudin sequence and integrin-directed cell attachment activity due to its RGD site. Our results suggest that this chimeric motif may serve as a prototype for a new class of anticoagulants where an integrin-specific sequence "targets" the peptide to a cell (ultimately through the platelet integrin alpha IIb beta 3) trapped amid a thrombus with ensuing proteinase inhibition.

Amino Acid Sequence↗
PubMed1987

Wool proteins of New Zealand Romney sheep.

Proteins extracted from the wool of 65 Romney ewes were analysed qualitatively by one- and two-dimensional polyacrylamide gel electrophoresis. Romney wool proteins could be classified into the low-sulfur, high-sulfur, and high-tyrosine protein groups described for wool from other breeds. The wool protein pattern of an individual sheep remained constant despite changes in season, age or nutritional status of the sheep, and did not vary between different body positions. There were between-sheep differences in protein pattern, most variation occurring in the high-sulfur protein group. These differences were presumed to reflect genetic differences between the sheep.

Animals↗