Bile acid acyl adenylate: a possible intermediate to produce a protein-bound bile acid.
Bile acid acyl adenylate: a possible intermediate to produce a protein-bound bile acid.
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胆汁酸酰基腺苷酸：生产蛋白质结合胆汁酸的可能中间体。
DOI：
--
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发表时间：
2001
影响因子：
2
通讯作者：
Reiko Kiyonami
中科院分区：
文献类型：
--
作者：
Junichi Goto;Masanori Nagata;N. Mano;Norihiro Kobayashi;Shigeo Ikegawa;Reiko Kiyonami
描述了通过胆汁酸的酰基腺苷酸的作用非酶促产生蛋白结合加合物。在磷酸盐缓冲液中与P物质一起孵育脱氧胆酰腺苷酸时，检测到与一个或两个胆汁酸分子共价结合的肽。修饰后的肽的结构进行了表征，通过飞行时间质谱与基质辅助激光解吸/电离（MALDI-TOFMS）在源后衰变模式，并通过液相色谱/电喷雾电离MS/MS。脱氧胆酸结合在物质P上通过氨基在Arg-1和/或Lys-3。胆酸的腺苷酸在与溶菌酶孵育时也产生蛋白结合的胆汁酸，并且胆酸的结合位点似乎是在1、33、97和116处的赖氨酸残基。结果清楚地表明，胆汁酸腺苷酸酯在体内可能作为活性中间体，通过游离氨基亲核置换5 '-腺苷酸，与肽和蛋白质共价结合胆汁酸加合物。
The non-enzymatic production of a protein-bound adduct by the action of the acyl adenylate of bile acids is described. On incubation of deoxycholyl adenylate with substance P in phosphate buffer, peptides covalently bound with one or two molecules of the bile acid were detected. The modified peptides were structurally characterized by time-of-flight mass spectrometry with matrix-assisted laser desorption/ionization (MALDI-TOFMS) in the post-source decay mode, and by liquid chromatography/electrospray ionization MS/MS. The deoxycholic acid was bound on substance P through the amino group at Arg-1 and/or Lys-3. The adenylate of cholic acid also produced the protein-bound bile acid on incubation with lysozyme, and the binding sites of the cholic acid appeared to be the lysine residues at 1, 33, 97 and 116. The results clearly suggest that bile acid adenylates in vivo may act as active intermediates to produce covalently bound bile acid adducts with peptides and proteins by nucleophilic displacement of the 5'-adenylic acid through the free amino groups.
串联质谱法应用于蛋白质结构问题。
影响因子：
3.9
作者：
Biemann,K
通讯作者：
Biemann,K
结肠癌和结肠息肉患者的组织胆汁酸。
DOI：
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发表时间：
1982
期刊：
The American journal of gastroenterology
影响因子：
--
作者：
Gelb,AM;McSherry,CK;Sadowsky,JR;Mosbach,EH
通讯作者：
Mosbach,EH
2-丙基戊酸活化过程中形成游离酰基腺苷酸。
DOI：
--
发表时间：
1992
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Mao,LF;Millington,DS;Schulz,H
通讯作者：
Schulz,H