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通过环孢素A的酸水解裂解获得的开链肽。

Open-chain peptides obtained by acidic hydrolytic cleavage of cyclosporin A.

作者信息

Magni F, Arcelloni C, Paroni R, Fermo I, Bonini P A, Del Puppo M, Manzocchi A, Galli Kienle M

机构信息

Scientific Institute H. S. Raffaele, Milan, Italy.

出版信息

Biol Mass Spectrom. 1994 Aug;23(8):514-8. doi: 10.1002/bms.1200230809.

Abstract

Hydrolysis of cyclosporin A (CsA) was studied in order to clarify the still undefined point of attack of the acidic degradation. Among ether extractable and water-soluble products formed from CsA in HCl, two open-chain peptides were isolated by high-performance liquid chromatography which were identified as the deca- and nonapeptides deriving from CsA through the hydrolytic cleavage of amino acid residue 11 and both residues 11 and 10, respectively. Identification was carried out by fast atom bombardment tandem mass spectrometry.

摘要

为了阐明环孢素A(CsA)酸性降解中仍未明确的攻击点,对其水解过程进行了研究。在盐酸中由CsA形成的醚提取物和水溶性产物中,通过高效液相色谱法分离出两种开链肽,分别鉴定为通过氨基酸残基11以及残基11和10的水解裂解而衍生自CsA的十肽和九肽。通过快速原子轰击串联质谱法进行鉴定。

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