• Transactions of the Korean Society of Mechanical Engineers A
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• v.37 no.2
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• pp.279-285
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• 2013

The feasibility of substituting a composite mold for an aluminum mold in the fabrication of a small ship propeller was investigated. A small three-blade aluminum propeller was used as a plug for manufacturing the composite mold. A GRPG composite mold and propeller were made from an unsaturated polyester resin, Epovia gelcoat, and woven and mat glass fibers using the compression and vacuum method at room temperature. The hardness and surface roughness and the strength and deformation of the compression and suction molds were experimentally determined. The results were compared with the ISO 484/2 standard and some aluminum alloy materials. The results showed that the deformation of the mold satisfied the tolerance of the thickness of the blade. Some characteristics of the GRPG composite mold were better than those of the aluminum alloy mold (surface smoothness, weight, performance, and cost), and some characteristics were similar (detachment ability and life-cycle). Therefore, the composite mold is considered suitable for the fabrication of a small composite ship propeller.

• The Korean Journal of Zoology
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• v.38 no.2
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• pp.167-176
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• 1995

Glucose-regulated proteins (grp's), srp94 3nd grp78/BiP, are a group of stress proteins which are highly synthesized in cells exposed to a variety of stressful agents including tunicamycin 3nd Ca2+ ionophore. Grp78/BiP is hon to function as a molecular chaperone which regulates the folding and assembly of secretory or membrane proteins, but the biological function of grp941 remains to be elucidated. In this study, we have examined the intracellular distribution of grV's and the function of srp94. Grp's are resident in the endoplasmic reticulum (ERI 3nd a specific sequence (Lys-Asp-Glu-Leu) at their C-terminus is known to be responsible for their retention within the ER. However, it has been unclear whether upon disturbance of cellular Caa+ homeostasis by the Ca2+ ionophore, grp94 is retained within the ER or secreted into the medium. In this study, we showed that in the presence of C3a+ ionophore, grp94 and gif78/BiP are present in the cells, mainly within the ER. We have also investigated whether grp94 might function as a molecular chaperone. Here we showed that in the immunoglobulin (Ig)-secreting hvbridom3 cells, grp94 transientlY interacts with fully glycosylated Is heavy chain, suggesting that grpg94 may be involved in facilitating the folding and assembly of Ig heavy chains.