Rose K, Savoy L A, Thim L, Christensen M, Jørgensen K H
Département de Biochimie Médicale, C.M.U. Geneva, Switzerland.
Biochim Biophys Acta. 1989 Oct 19;998(3):297-300. doi: 10.1016/0167-4838(89)90288-4.
The published amino acid sequence of pancreatic spasmolytic polypeptide (Thim, L., Thomsen, J., Christensen, M. and Jørgensen, K.H. et al. (1985) Biochim. Biophys. Acta 827, 410-418) has been checked by a combination of mass spectroscopy and Edman degradation. The pyroglutamyl blocking group was positively identified, and residue assignments at four positions were corrected: Lys48 (not Ser), Ser63 (not Lys), Cys68 (not Ser) and Ser74 (not Cys). The revised sequence exhibits greater similarity with pS2 peptide, a 60 residue polypeptide which is induced by oestrogen in the human breast cancer cell line MCF-7 and found in malignant but not in non-malignant breast tissue.
胰腺解痉多肽已发表的氨基酸序列(蒂姆,L.,汤姆森,J.,克里斯蒂安森,M.和乔根森,K.H.等人(1985年),《生物化学与生物物理学学报》827卷,410 - 418页)已通过质谱和埃德曼降解相结合的方法进行了核对。焦谷氨酰封闭基团得到了明确鉴定,四个位置的残基归属得到了校正:赖氨酸48(不是丝氨酸)、丝氨酸63(不是赖氨酸)、半胱氨酸68(不是丝氨酸)和丝氨酸74(不是半胱氨酸)。修订后的序列与pS2肽有更高的相似性,pS2肽是一种由雌激素在人乳腺癌细胞系MCF - 7中诱导产生、在恶性乳腺组织而非良性乳腺组织中发现的60个残基的多肽。