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Breaking the Adhesive Bond between Dialyll Phthlate, Barco Bond 185 and PBX 9501
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作者 Matt Jackson Benton Allen +4 位作者 Trent Kelly Courtney Waddell Emily M. Hunt Stephanie Steelman Neil Koone 《Journal of Materials Science and Chemical Engineering》 2015年第7期196-201,共6页
Use of epoxy as an adhesive is a common practice. The most common applications are permanent sealants. Epoxies have a wide range of operating temperatures, and are very resistance to adhesive failure. When a need to r... Use of epoxy as an adhesive is a common practice. The most common applications are permanent sealants. Epoxies have a wide range of operating temperatures, and are very resistance to adhesive failure. When a need to remove this adhesive arises, it is not always easily accomplished especially if the part has excessive adhesive. To maintain fidelity of the parts attached by epoxy, a project evaluating several methods of epoxy removal was conducted. Methods evaluated included low wavelength, near-ultraviolet radiation, solvent dissolution, and thermal cycling. The UV method failed to demonstrate a repeatable dissociation. The solvent study did result in dissociation of bonds, but introduced chemicals that could make subsequent chemical analysis of parts suspect. Thermal cycling showed a high repeatability for dissociation of bonds and may prove to be relatively inexpensive to implement. 展开更多
关键词 BARCO BOND BOND DISSOCIATION Cyrogenic CYCLING Dialyll Phthlate EPOXY BOND EPOXY degredation EPOXY DISSOCIATION Thermal CYCLING PBX 9501 Plastic Bonded Explosive
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AProteinase Responsible for Degrading Yolk Proteins in Tussah(Antheraea pernyi)
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作者 赵小凡 王金星 《Developmental and Reproductive Biology》 1994年第1期37-41,T001,共6页
A proteinase responsible for degradation of yolk proteins has been discovered in oocyte of Antheraea pernyi which was found to found to hydrolyze vitelluin effectively in acidic pH. Using bovine hemoglobin as substrat... A proteinase responsible for degradation of yolk proteins has been discovered in oocyte of Antheraea pernyi which was found to found to hydrolyze vitelluin effectively in acidic pH. Using bovine hemoglobin as substrate,the optimum pH was determine3d at 3.5.Unaffected by EDTA and DipF, the activity of the proteinase was strongly inhibited by E64 and other thiol blocking reagents. It is thus very likely to be a cysteine proteinase. Activity of the proteinas. was found to be increasing in developing oocyte. 展开更多
关键词 Antheraea pernyi Yolk proteins Degredative proteinase.
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