Böhme I, Hütter H J, Gerlach W, Haschen R J
Enzyme. 1976;21(5):464-70. doi: 10.1159/000458895.
Alanine aminopeptidase (particle-bound aminopeptidase, EC 3.4.11.2) isolated in a highly purified state from human liver, kidney, and pancreas were investigated with regard to their different electrophoretic mobilities. While the molecular weights are identical, different isoelectric points were found. The results of carbohydrate analysis point to N-acetylneuraminic acid as the main factor that causes the differences in electrophoretic behaviour of the alanine aminopeptidases investigated.
对从人肝脏、肾脏和胰腺中高度纯化分离得到的丙氨酸氨基肽酶(颗粒结合氨基肽酶,EC 3.4.11.2)的不同电泳迁移率进行了研究。虽然分子量相同,但发现了不同的等电点。碳水化合物分析结果表明,N-乙酰神经氨酸是导致所研究的丙氨酸氨基肽酶电泳行为差异的主要因素。