Vendrell J, Avilés F X, Genescà E, San Segundo B, Soriano F, Méndez E
Biochem Biophys Res Commun. 1986 Dec 15;141(2):517-23. doi: 10.1016/s0006-291x(86)80203-0.
The complete primary structure of the activation segment of monomeric procarboxypeptidase A from porcine pancreas has been determined by automated and manual Edman-like degradation methods performed on its fragments generated by enzymatic cleavage. The polypeptide consists of 94 residues, with a molecular mass of 10,768, and presents a high proportion of acidic and hydrophobic residues and a proline-rich region in the center of the molecule. Comparison of this sequence with the already reported equivalent sequence deduced from rat procarboxypeptidase A cDNA reveals a very high degree of homology between the two propeptides (up to a 81% of identities), which is even higher in certain large zones of the molecule.
通过对猪胰腺单体羧肽酶原A激活片段经酶切产生的片段进行自动化和类似埃德曼降解的手动降解方法，已确定其完整的一级结构。该多肽由94个残基组成，分子量为10768，分子中酸性和疏水残基比例较高，且在分子中心有一个富含脯氨酸的区域。将该序列与已报道的从大鼠羧肽酶原A cDNA推导的等效序列进行比较，发现两种前肽之间具有非常高的同源性（同一性高达81%），在分子的某些大区域甚至更高。
