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Myosin antibody preparation

Various antibody preparations have been developed that facilitate imaging of vascular-related conditions, including myocardial infarction, deep vein thrombosis and atherosclerosis. Anti-myosin monoclonal antibody fragments (Fab) labelled with mIn, for example, have been used for imaging purposes in conjunction with a planar gamma camera. The antibody displays specificity for intracellular cardiac myosin, which is exposed only upon death of heart muscle tissue induced by a myocardial infarction (heart attack). [Pg.395]

ATP cannot be effectively delivered to most tissues including the ischemic myocardium without protection from degradation by plasma endonucleotidases. However, it has been established that ATP can be delivered to various tissues by its encapsulation within liposomal preparations. We describe here, the materials needed and methods used to optimize the encapsulation of ATP in liposomes, enhance their effectiveness by increasing their circulation time and target injured myocardial cells with Uposomal siufece anti-myosin antibody. Additionally, we outline methods for ex vivo studies of these ATP liposomal preparations in an isolated ischemic rat heart model and for in vivo studies of rabbits with an induced myocardial infarction. The expectation is that these methods will provide a basis for continued studies of effective ways to deliver energy substrates to the ischemic myocardium. [Pg.361]

ATP-immunoliposomes (ATP-IL) are prepared using the micelle transfer method by modification of the ATP-L with anti-myosin antibody 2G4. [Pg.367]

A EXPERIMENTAL FIGURE 19-20 Fluorescent antibodies reveal the localization of myosin I and myosin II during cytokinesis. Fluorescence micrograph of a Dictyostelium ameba during cytokinesis reveals that myosin II (red) is concentrated in the cleavage furrow, whereas myosin I (green) is localized at the poles of the cell. The cell was stained with antibodies specific for myosin I and myosin II, with each antibody preparation linked to a different fluorescent dye. [Courtesy ofY Fukui.j... [Pg.796]

Purification of detergent-solubilized la antigens Isolation of a-o-mannosidase from jack bean by affinity chromatography Preparation of specific anti-(unc 54-myosin) antibodies by immunoadsorption Affinity chromatography of glycosidases... [Pg.632]

For these experiments, they used a more well-defined method for attaching the myosin to the beads. The beads were clumps of killed bacterial (Staphylococcus aureus) cells. These cells have a protein on their surface that binds to the Fc region of antibody molecules (Fig. 5-2la). The antibodies, in turn, bind to several (unknown) places along the tail of the myosin molecule. When bead-antibody-myosin complexes were prepared with intact myosin molecules, they would move along Nitella actin fibers in the presence of ATP. [Pg.60]

Spudich and colleagues prepared bead-antibody-myosin complexes with varying amounts of myosin, HMM, and SHMM, and measured their speeds along Nitella actin fibers in the presence of ATP. The graph below sketches their results. [Pg.61]

Starr and Offer (1971) examined the SDS—gel electrophoresis patterns of conventional myosin preparations and pointed out the presence of several unknown protein bands other than myosin heavy and light chains. As a result, C (135 kDa), F (121 kDa), and H (74 kDa) proteins have been isolated and shown to be myosin-associated proteins. The C protein, discovered by Offer et al. (1973), is localized to seven regularly spaced stripes in each half of the A bands of rabbit psoas muscle (Craig and Offer, 1976), and studies using monoclonal antibodies have shown... [Pg.3]


See other pages where Myosin antibody preparation is mentioned: [Pg.269]    [Pg.136]    [Pg.136]    [Pg.31]    [Pg.9]    [Pg.165]    [Pg.5]    [Pg.14]    [Pg.136]    [Pg.632]   
See also in sourсe #XX -- [ Pg.5 ]




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