Hopwood D, Yeaman G, Milne G
Department of Pathology, Ninewells Hospital and Medical School, Dundee, UK.
Histochem J. 1988 Jun-Jul;20(6-7):341-6. doi: 10.1007/BF01002727.
Alkaline phosphatase activity in mouse liver blocks, cooled by an ice-bath, decreased by 50% in 5 min of microwave irradiation (280 W). This loss of protein tertiary structure has been mirrored by ultrastructural changes in the same tissue. Microwave irradiation did not produce cleavage or polymerization of lysozyme or haemoglobin. Protein formaldehyde reaction mixtures produced protein polymers between 0 degree and 40 degrees C which could be separated by SDS-polyacrylamide gel electrophoresis. Microwave irradiation of lysozyme or haemoglobin plus formaldehyde on ice-bath up to 30 min produced a similar electrophoretic pattern. When lysozyme or haemoglobin plus formaldehyde was heated to 60 degrees C for 30 min, the protein polymers migrated faster on electrophoresis, suggesting a smaller hydrodynamic volume than expected due to intramolecular crosslink formation, not opened up under the conditions of electrophoresis.
用冰浴冷却的小鼠肝脏组织块中的碱性磷酸酶活性，在280瓦微波照射5分钟后降低了50%。相同组织中的超微结构变化反映了蛋白质三级结构的这种损失。微波照射未导致溶菌酶或血红蛋白的裂解或聚合。蛋白质甲醛反应混合物在0℃至40℃之间产生蛋白质聚合物，这些聚合物可用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分离。在冰浴上对溶菌酶或血红蛋白加甲醛进行长达30分钟的微波照射，产生了相似的电泳图谱。当溶菌酶或血红蛋白加甲醛加热至60℃ 30分钟时，蛋白质聚合物在电泳中迁移得更快，这表明由于分子内交联形成，其流体力学体积比预期的小，在电泳条件下未展开。
