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Biomedical subjects

B F Edwards

Publications and source records attributed to B F Edwards.

At least 73 records · Page 4Linked to original sources
PubMed1979

Comparative tumor-inhibitory and anti-bacterial activity of soluble and particulate glucan.

A soluble fraction of particulate glucan was prepared and evaluated for its anti-tumor and anti-bacterial activity. Thin-layer chromatographic analysis indicated that the soluble preparation was composed of a variety of polyglucoses. Intravenous administration of soluble or particulate glucan resulted in significant reductions in the growth of a syngeneic anaplastic mammary carcinoma and melanoma B16. Survival data demonstrated that intravenous administration of soluble or particulate glucan prolonged survival of A/J and C57BL/6J mice with subcutaneous tumor implants. As regards to bacterial infections, soluble and particulate glucan decreased renal necrosis in S. aureus challenged mice as compared to control mice. Although the exact nature of the active soluble fraction(s) of glucan remains to be delineated, these studies demonstrate that a soluble glucan preparation exhibits significant anti-tumor and anti-staphylococcal activity. The active soluble fraction of particulate glucan may be preferable to particulate glucan in view of the inherent ease of parenteral administration.

Animals↗
PubMed1977

Chronic acceleration in plants.

Since this subject was last reviewed (at the Symposium on Gravity and the Organism, 1967), relatively little new work on hypergravity effects on plants has appeared. Centrifugation has been used widely for separation of cellular components, but only occasionally as a primary environmental condition. With increasing magnitude of accelerative forces, the following effects have been reported by a number of authors working with many different plants. In the range 2-25 g, auxin transport and geotropic response in coleoptiles are increased and growth is stimulated. From 25 to 500 g, coleoptile growth is reduced and some morphological changes may be seen. At 1000-2500 g, root formation in willow cuttings increases. From 1000 g upward, cytoplasmic stratification occurs and seed germination decreases. Between 200 and 15000 g, chromosome damage has been observed. Algal cell polarity may be reversed at 5000 to 20000 g. Above 30000 g, the response of some cells to gibberellic acid is halted. Permanent morphologic changes in Escherichia coli are produced at 110000 g. Some plant cells have survived 176000 g for 20 hr.

Acceleration↗
PubMed1974

Complex of aspartate carbamoyltransferase from Escherichia coli with its allosteric inhibitor, cytidine triphosphate: electron density at 5.9-angstroms resolution.

Following our earlier determination of the three-dimensional structure of aspartate carbamoyltransferase (EC 2.1.3.2; carbamoylphosphate: L-aspartate carbamoyltransferase) to 5.5-A resolution [S. G. Warren, B. F. P. Edwards, D. R. Evans, D. C. Wiley & W. N. Lipscomb (1973) Proc. Nat. Acad. Sci. USA 70, 1117-1121], we report here, from a different crystal form, the three-dimensional structure at 5.9 A of this enzyme complexed with its allosteric inhibitor, cytidine triphosphate. Location of the major binding site of this inhibitor within each of the six regulatory chains is made secure by comparison of these results with those obtained upon binding of 5-iodocytidine triphosphate to the enzyme. Conformational changes in the aspartate carbamoyltransferase molecule when this inhibitor binds are described briefly at 5.9-A resolution.

Allosteric Regulation↗
PubMed1973

Aqueous central cavity in aspartate transcarbamylase from Escherichia coli.

A three-dimensional x-ray diffraction study of aspartate transcarbamylase to 5.5-angstrom resolution, with the aid of four isomorphous heavy atom derivatives, indicates the presence of a central aqueous cavity approximating an oblate spheroid about 25 by 50 by 50 angstroms in dimension, within a molecule about 90 by 110 by 110 angstroms in largest dimensions.

Aspartate Carbamoyltransferase↗
PubMed1973

Aspartate transcarbamoylase from Escherichia coli: electron density at 5.5 A resolution.

The allosteric enzyme, aspartate transcarbamoylase (EC 2.1.3.2), has previously been shown in our x-ray diffraction studies to have D(3)-32 symmetry. There are six catalytic (C) and six regulatory (R) chains in the molecular complex (R(6)C(6)). Our three-dimensional x-ray diffraction study of this enzyme (R32, a = 131 A, c = 200 A) at 5.5 A resolution shows a spatial arrangement of the two catalytic trimers C(3) above and below an equatorial belt of three regulatory dimers R(2). The molecule is about 110 x 110 x 90 A in largest dimensions, and is shown here to contain a large central aqueous cavity about 50 x 50 x 25 A in size. Location of the single sulfhydryl of each catalytic chain, and correlation of its reactivity with enzymatic activity in the molecule, suggests that the nearby active sites are most probably accessible from the central cavity, but probably not directly from the external solution. The most obvious access to the central cavity consists of six channels, each about 15 A in diameter, near the regulatory region. A component of the regulatory mechanism may be modulation of access of substrates through these channels.

Allosteric Regulation↗