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Biomedical subjects

F M Clarke

Publications and source records attributed to F M Clarke.

52 records · Page 3Linked to original sources
PubMed1979

Changes associated with glycolytic-enzyme binding in the equatorial X-ray-diffraction pattern of glycerinated rabbit psoas muscle.

The binding of fructose biphosphate aldolase to the thin filaments of glycerinated rabbit psoas muscle produces a significant change in its low-angle X-ray-diffraction pattern. The intensity of the (11) reflection relative to that of the (10) reflection increases by 26 +/- 3% (mean +/- S.E.M.), which is consistent with the increase in the mass of the thin filaments produced by enzyme binding. A similar effect is found with a mixture of aldolase and glyceraldehyde 3-phosphate dehydrogenase. The significance of the change in intensity is considered with reference to the interpretation of the equatorial patterns obtained from muscles in different physiological states. The magnitude of the increase in the relative intensity of the (11) reflection is lower than that observed between relaxed and contracting muscle and does not bring into question the interpretation linking changes in these patterns to cross-bridge movement. However, the effect due to enzyme binding may be important when making detailed interpretations of these changes. It may also be related to an unusual pattern sometimes observed in cardiac muscle.

Animals↗
PubMed1978

Detection and separation of two serum factors responsible for depression of lymphocyte activity in pregnancy.

Studies using the rosette inhibition test have demonstrated a depression of lymphocyte activity in pregnant mice which occurs as early as 6 hr after fertilization and persists until just before delivery. This depression of lymphocyte activity is induced by two serum factors, the relative contributions of which vary with the time of gestation. The first, a high molecular weight early pregnancy factor, appears within hours of fertilization and then slowly declines in activity as gestation proceeds. The second, a lower molecular weight substance which cross-reacts with antiserum to human chorionic gonadotrophin, appears after the formation of the trophoblast at 4--5 days and persists until parturition.

Animals↗
PubMed1977

Modification of the kinetic parameters of aldolase on binding to the actin-containing filaments of skeletal muscle.

The kinetic parameters of fructose bisphosphate aldolase (EC 4.1.2.13) were shown to be modified on binding of the enzyme to the actin-containing filaments of skeletal muscle. Although binding to F-actin or F-actin-tropomyosin filaments results in relative minor changes in kinetic properties, binding to F-actin-tropomyosin-troponin filaments produces major alterations in the kinetic parameters, and, in addition, renders them Ca2+-sensitive. These observations may be relevant to an understanding of the function of this enzyme within the muscle fibre.

Actins↗
PubMed1977

An electron microscope study of the interaction between fructose diphosphate aldolase and actin-containing filaments.

The interaction of fructose diphosphate aldolase with F-actin, F-actin-tropomyosin, and F-actin-tropomyosin-troponin has been studied by using negative staining. In the absence of troponin, minor aggregates of aldolase and the F-actin filaments are formed. A well-ordered lattice structure is only formed in the case of the fully reconstituted filament when the filament-to-filament spacing is 18nm, and the cross-bridge spacing is 38.7 nm. Evidence is presented that the lattice is due to an interaction between troponin and aldolase. The minimum subunit structure of troponin, still capable of giving rise to a lattice, is the troponin-IT complex, which indicates that troponin-C is not involved in aldolase binding.

Actins↗
PubMed1977

Multiple myeloma and monoclonal IgA with anti-actin reactivity.

Serum containing a monoclonal IgA protein from a patient with multiple myeloma gave intense immunofluorescent staining of smooth muscle fibres and the striations of skeletal muscle, cardiac muscle and thymic myoid cells. It also gave a weaker reaction with hepatocytes in a 'polygonal' pattern, and with renal glomeruli in a diffuse pattern. In culture fibroblasts, the serum stained long, parallel cytoplasmic filaments. Specificity of the staining reactions for actin was established by their prevention on serum absorption with skeletal muscle actin, but not by skeletal muscle myosin, tropomyosin or troponin, and by the demonstration that eluates obtained by acid dissociation of the serum-actin precipitates gave the same staining reactions as the original serum. Localization of the anti-actin reactivity to the monoclonal IgA protein was established by the observation that the same staining reactions were obtained with a monospecific IgA conjugate, with the eluate derived from the gamma globulin band of a serumel ectrophoretic strip, and with a purified euglobulin (IgA) fraction; also, the eluates obtained by acid dissociation of the serum actin precipitates contained monoclonal IgA.

Actins↗
PubMed1976

Aldolase binding to actin-containing filaments. Formation of paracrystals.

Electron-microscopy observation show that when aldolase binds to F-actin or F-actin-tropomyosin, highly ordered paracrystalline structures are formed consisting of tightly packed filament bundles cross-banded at 36 nm intervals. Morphologically different paracrystalline arrays are formed between aldolase and F-actin-tropomyosin-troponin. The filament bundles are far more extensive and are characterized by a prominent cross-striation at 38nm intervals. It is suggested that this reflects an interaction between troponin and aldolase.

Actins↗
PubMed1976

Beef muscle troponin: evidence for multiple forms of troponin-T.

A method is described for the purification of troponin from beef skeletal muscle. The resultant preparation differs from the troponin of rabbit skeletal muscle in that it contains at least two forms of the tropomyosin-binding component, Troponin-T: these are designated as the 37 000 and 40 000 dalton forms of Troponin-T on the basis of sodium dodecyl sulphate gel electrophoresis. Either of these Troponin-T forms may be used to reconstitute troponin by mixing with the appropriate amounts of the calcium-binding (Troponin-C) and and actomyosin ATPase-inhibitory (Troponin-I) components. These reconstituted troponins are shown to interact with tropomyosin and also to confer full calcium sensitivity on actomyosin ATPase. Despite the existence of proteolysis in troponin preparations, the experimental evidence indicates that the smaller form of Troponin-T is not derived from the 40 000 dalton species by limited degradation. Although both species of Troponin-T have been found routinely in troponin from beef skeletal muscle, only the larger form is detected in troponin preparations from beef cardiac muscle. Further studies are required in order to clarify the functional significance and differential distribution of these multiple forms of Troponin-T.

Actomyosin↗
PubMed1975

On the association of glycolytic enzymes with structural proteins of skeletal muscle.

1. The effects of protein concentration and ionic strength on the adsorption of the individual glycolytic enzymes to F-actin and F-actin--trypomyosin--troponin have been studied. 2. Appreciable association was demonstrated under conditions of physiological ionic strength and high protein concentration, and tropomyosin--troponin established as an important and generalized component of these interactions. 3. Phosphofructokinase, aldolase, pyruvate kinase, lactate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase and glucose-6-phosphate isomerase were strongly bound under these conditions, while triosephosphate isomerase, phosphoglycerate kinase, phosphoglycerate mutase, enolase and hexokinase displayed less adsorption to the structural proteins. 4. The influence of a number of parameters on the adsorption phenomena was examined. Ca2+ and fructose 1,6-diphosphate increased the adsorption of aldolase, lactate dehydrogenase and pyruvate kinase, while decreasing the adsorption of the enzymes of the constant-proportion group. 5. Of the other major enzymic components of skeletal muscle, creatine kinase, adenylate kinase and malate dehydrogenase showed no adsorption to F-actin--tropomyosin--troponin under the experimental conditions. Some adsorption was evident, however, in the case of aspartate aminotransferase, (NADP) isocitrate dehydrogenase and alpha-glycerolphosphate dehydrogenase. 6. These results have been discussed in relation to their functional significance and the roles of enzyme compartmentation in the cell.

Animals↗
PubMed1974

Interaction of aldolase with the troponin-tropomyosin complex of bovine muscle.

Ultracentrifugal studies of mixtures of aldolase and the troponin-tropomyosin complex from bovine muscle showed the existence of a labile interaction between these two myofibrillar constituents in imidazole buffers, pH6.8, I 0.02-0.10 (mol/l), and the suppression of the reaction by fructose 1,6-diphosphate. Analysis of the sedimentation-velocity patterns suggests the binding of more than 2 molecules of troponin-tropomyosin/molecule of aldolase. The results illustrate the necessity of considering additional or alternative sites to F-actin to account for the observed binding of aldolase to the thin filaments of skeletal muscle.

Actins↗