Harwig S S, Kokryakov V N, Swiderek K M, Aleshina G M, Zhao C, Lehrer R I
Department of Medicine, UCLA School of Medicine 90095, USA.
FEBS Lett. 1995 Mar 27;362(1):65-9. doi: 10.1016/0014-5793(95)00210-z.
We purified and characterized an unusual antimicrobial peptide, prophenin-1 (PF-1), from porcine leukocytes. The peptide had a mass of 8,683 and contained 79 residues, including 42 (53.2%) prolines and 15 (19.0%) phenylalanines. Its N-terminal 60 residues consisted of three perfect and three nearly perfect repeats of a decamer, FPPPNFPGPR. Prophenin-1 was encoded on a cathelin-containing precursor and showed substantially more activity against E. coli, a Gram-negative bacterium, than against Listeria monocytogenes, a Gram-positive organism, in vitro.
我们从猪白细胞中纯化并鉴定了一种不寻常的抗菌肽——前菌素-1（PF-1）。该肽的质量为8683，含有79个氨基酸残基，其中包括42个（53.2%）脯氨酸和15个（19.0%）苯丙氨酸。其N端的60个残基由一个十肽FPPPNFPGPR的三个完美重复序列和三个近乎完美的重复序列组成。前菌素-1由一个含组织蛋白酶原的前体编码，在体外对革兰氏阴性菌大肠杆菌的活性比对革兰氏阳性菌单核细胞增生李斯特菌的活性要强得多。
