Molecular cloning and identification of a novel porcine cathelin-like antibacterial peptide precursor.

B Strukelj, J Pungercar, G Kopitar, M Renko, B Lenarcic, S Berbić, V Turk
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引用次数: 23

Abstract

A novel clone (C6) encoding the precursor of a 79-residue proline/arginine-rich antibacterial peptide prophenin was isolated from a porcine bone marrow cDNA library. Its deduced N-terminal propart shows 84% identity with cathelin. Additionally, two cathelin isoforms were isolated from peripheral porcine blood and their N-termini sequenced. The sequence of one isoform corresponds to the cathelin sequence, whereas that of the other protein is identical to the propeptide of C6 clone. Western blot analysis of total proteins from porcine and human bone marrow using polyclonal antibodies against cathelin revealed the presence of immunochemically related high molecular mass proteins of about 30 kDa in both samples, whereas low molecular mass proteins of approximately 12 kDa, corresponding to isolated cathelin, were not detected in human bone marrow.

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一种新型猪cathelin样抗菌肽前体的分子克隆与鉴定。
从猪骨髓cDNA文库中分离到一个富含脯氨酸/精氨酸的抗菌肽prophenin前体的克隆(C6)。其推断的n端比例与cathelin的一致性为84%。此外,从猪外周血中分离到两个cathelin亚型,并对它们的n端序列进行了测定。其中一个同工异构体的序列与cathelin序列一致,而另一个同工异构体的序列与C6克隆的前肽相同。用抗cathelin的多克隆抗体对猪和人骨髓的总蛋白进行Western blot分析,发现两种样品中都存在约30 kDa的免疫化学相关的高分子质量蛋白,而在人骨髓中未检测到约12 kDa的低分子质量蛋白,与分离的cathelin相对应。
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