Petrelli C, Moretti P, Petrelli F, Barra D
Dipartimento di Biologia Molecolare, Cellulare e Animale, Università di Camerino.
Ital J Biochem. 1992 May-Jun;41(3):170-82.
A low molecular factor showing high specific activity in the control DNA of transcription in vitro was isolated from aqueous ultrafiltered calf pineal gland extracts. The active factor was purified by means of Gel filtration on Sephadex G-25 and G-10, thin layer chromatography on aluminum sheet cellulose and high performance liquid chromatography using a Supelcosil LC 318 reverse phase column. The purified pineal factor was characterized as a peptide of low molecular weight (of about 1200 Dalton) containing glutamic acid, leucine, glycine, threonine and alanine in their approximate molar ratio, referred to glycine taken as 1: glycine 1, threonine 1, leucine 1, alanine 6, glutamic acid 2. Studies of the aminoacid sequence by N-terminal analysis using the automated Edman degradation procedure, were unsuccessful, suggesting the presence of a blocked NH2 group. The purified peptide appears to be different from peptide factors till now isolated from pineal gland.
从超滤后的小牛松果体水提取物中分离出一种在体外转录的对照DNA中显示出高比活性的低分子因子。通过在Sephadex G - 25和G - 10上进行凝胶过滤、在铝板纤维素上进行薄层色谱以及使用Supelcosil LC 318反相柱进行高效液相色谱法对活性因子进行了纯化。纯化后的松果体因子被鉴定为一种低分子量肽（约1200道尔顿），其谷氨酸、亮氨酸、甘氨酸、苏氨酸和丙氨酸的摩尔比近似为：以甘氨酸为1时，甘氨酸1、苏氨酸1、亮氨酸1、丙氨酸6、谷氨酸2。使用自动埃德曼降解程序通过N端分析对氨基酸序列进行研究未成功，这表明存在一个被封闭的NH2基团。纯化后的肽似乎与目前从松果体中分离出的肽因子不同。
