Tanaka Y, Uritani I
J Biochem. 1976 Jan;79(1):217-9. doi: 10.1093/oxfordjournals.jbchem.a131049.
Antibody toward phenylalanine ammonia-lyase (PAL) [EC 4.3.1.5] was obtained by immunization of a rabbit with highly purified PAL. The antibody reacted specifically with RAL, as demonstrated by the Ouchterlony double diffusion test, immunoelectrophoresis, and SDS polyacrylamide gel electrophoresis of the immunoprecipitate. Experiments using anti-PAL showed that PAL was not present in fresh sweet potato tissue, but appeared in response to cut injury, reaching a maximum, and then decreasing, in parallel with PAL activity. The results suggest that the development of PAL activity was due to de novo synthesis of PAL and that the decrease of PAL activity after reaching a maximum was due to proteolytic degradation of PAL.
通过用高度纯化的苯丙氨酸解氨酶（PAL）[EC 4.3.1.5]免疫兔子获得了抗PAL抗体。如免疫沉淀的琼氏双扩散试验、免疫电泳和SDS聚丙烯酰胺凝胶电泳所示，该抗体与RAL特异性反应。使用抗PAL的实验表明，新鲜甘薯组织中不存在PAL，但在受到切割损伤后出现，达到最大值，然后下降，与PAL活性平行。结果表明，PAL活性的增加是由于PAL的从头合成，而PAL活性达到最大值后下降是由于PAL的蛋白水解降解。
