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Biomedical subjects

P R Andrews

Publications and source records attributed to P R Andrews.

7 recordsLinked to original sources
PubMed1992

Motion reveals spatial visual defects.

The question of how we can be unaware of the deficit in our (monocular) visual field, equivalent in size to 76 full moons, is examined. A new method of investigating the response to moving images on and near the blind spot has been found. The image of a computer-generated line, which is made to lengthen with time and pass over the blind spot, is seen as shorter than that of a similar, parallel line which passes outside the blind spot. This perceived difference in length corresponds to the actual width of the blind spot. Our unawareness of blind spots and scotomata is often described as involving some form of 'filling in' process. The rapid variation in cortical receptive field size, recently found to occur in response to stabilized images, may provide a general filling-in mechanism for the removal from perception of otherwise-distracting, stabilizing image regions (such as the shadows of blood vessels and clinical scotomata).

Humans↗
PubMed1979

Convulsant, anticonvulsant and anaesthetic barbiturates. 5-Ethyl-5-(3'-methyl-but-2'-enyl)-barbituric acid and related compounds.

Barbiturates derived by minor structural changes to the butenyl sidechain of the convulsant 5-ethyl-5-(3'-methyl-but-2'-enyl)-barbituric acid are almost devoid of convulsant activity, but all have anaesthetic and anticonvulsant effects. Anticonvulsant activity is also observed in the convulsant barbiturate. Increased lipophilic character does not increase anaesthetic potency, only speed of onset, and anticonvulsant activity is reduced in the more lipophilic compounds. The stereochemistry at the 3'-position of the sidechain is vitally important to convulsant activity, and also influences anticonvulsant potency.

Anesthetics↗
PubMed1977

Rearrangement of chorismate to prephenate. Use of chorismate mutase inhibitors to define the transition state structure.

The enzymically catalyzed conversion of chorismate to prephenate may proceed through either a chair-like or a boat-like transition state. To distinguish between these alternatives, we have prepared a series of structural analogues of the two possible transition state structures and tested them as inhibitors of chorismate mutase-prephenate dehydrogenase from Escherichia coli K12. The results indicate that the enzymically catalyzed reaction passes through a chair-like intermediate. None of the compounds studied is an ideal transition state analogue; it seems likely that the partial bond structure of the transition state precludes the corresponding orientation of the side chain in stable molecules. Nevertheless, the new inhibitors are stronger than any previously available, and the degree of inhibition is consistent with bacteriostatic activity recently observed in some of the compounds.

Alkanes↗
PubMed1976

The use of sedimentation coefficients to distinguish between models for protein oligomers.

The sedimentation coefficients of proteins are dependent on their sizes, shapes and densities and on the density and viscosity of the solvent. However, when the sedimentation coefficients of an oligomeric protein and its protomer are measured under the same experimental conditions, the ratio of the two coefficients depends only on the protomer shape and the mode of aggregation. This property, which we shall call the sedimentation ratio, therefore provides a way of distinguishing between models for oligomeric proteins. To allow examination of the behaviour of the sedimentation ratio, sedimentation coefficients are calculated for a comprehensive range of protomer shapes and modes of aggregation in hexameric systems using equations derived by Kirkwood. As illustrations of the method the resulting sedimentation ratios are compared with experimental values for insulin and arthroped hemocyanin, which eliminates many of the possible structures for these proteins. When experimental estimates of degree of hydration and molecular dimensions are also considered, all but a group of virtually identical structures are eliminated for the insulin hexamer and a single most likely structure remains for arthropod hemocyanin. The insulin structure is in good agreement with that determined by X-ray crystallography while the hemocyanin hexameric structure is a hexagonal prism formed by the cyclic aggregation of prolate ellipsoids of axial ratio about 2.5 : 1.

Binding Sites↗