Linder D, Linder M, Schade H, Sziegoleit A
Biochemisches Institut am Klinikum der Justus-Liebig-Universität, Giessen, Germany.
Biomed Chromatogr. 1993 May-Jun;7(3):143-5. doi: 10.1002/bmc.1130070308.
Human pancreatic carboxypeptidase A, which was isolated from a pool of necrobiotic pancreae, crystallized spontaneously and appeared homogenous in sodium dodecylsulphate polyacrylamide gel electrophoresis. Reversed phase high performance liquid chromatography of the dissolved crystals, however, revealed the presence of two distinct isoenzymes, which were shown by aminoterminal sequence analysis to be only 61% homologous in their 31 amino terminal amino acids. On the other hand, amino terminal sequences of the isoenzymes were found to be 79% and 87% homologous with CAP1 and CPA2 of the rat, respectively. Thus, the presence of two distinct pancreatic carboxypeptidase A isoenzymes could be clearly demonstrated for the first time in human tissue.
从坏死胰腺池中分离出的人胰腺羧肽酶A能自发结晶，并且在十二烷基硫酸钠聚丙烯酰胺凝胶电泳中呈现均一性。然而，对溶解晶体进行反相高效液相色谱分析后发现存在两种不同的同工酶，通过氨基末端序列分析表明，它们在31个氨基末端氨基酸中只有61%的同源性。另一方面，发现这两种同工酶的氨基末端序列与大鼠的CAP1和CPA2分别有79%和87%的同源性。因此，首次在人体组织中明确证实了存在两种不同的胰腺羧肽酶A同工酶。
