360-MHz nuclear magnetic resonance and laser photochemically induced dynamic nuclear polarization studies of bile salt interaction with porcine colipase A.
360-MHz nuclear magnetic resonance and laser photochemically induced dynamic nuclear polarization studies of bile salt interaction with porcine colipase A.
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胆汁盐与猪辅脂肪酶 A 相互作用的 360 MHz 核磁共振和激光光化学诱导动态核极化研究。
DOI：
10.1111/j.1432-1033.1981.tb06181.x
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发表时间：
1981
期刊：
影响因子：
--
通讯作者：
Kaptein,R
中科院分区：
文献类型：
--
作者：
Cozzone,PJ;Canioni,P;Sarda,L;Kaptein,R
猪胰腺辅脂酶具有特定的三维表面结构域，其在高度疏水环境中含有分子的七个芳香族残基中的六个[P. Canioni和P. Cozzone（1979）Biochimie（巴黎）61，343-354; J. Wieloch，B. Borgström，K. E. Falk和S. Forsen（1979）Biochemistry，18，1622-1628]。该结构域对应于通过蛋白质折叠而空间接近的49-57和77-86 β折叠片段[P. Canioni，P. Cozzone和L. Sarda（1980）Biochim. Biophys. Acta，621，29-42].根据核磁共振和光化学诱导的动态核极化，提出了这一特定结构域作为辅脂酶上的脂质结合位点的鉴定（photo‐CIDNP）研究了辅脂酶与有机胆盐胶束的复合物。牛磺脱氧胆酸盐胶束的结合特异性地干扰了Tyr‐I和Tyr‐II的质子NMR环共振。（Tyr-56和Tyr-57）和His-II（His-86）以及几个脂肪族共振，反映了疏水芳族结构域参与胶束固定。在存在辅脂酶的情况下，观察到牛磺脱氧胆酸盐的甾烷环的位置18和21处的甲基的特定移位和加宽，并且表明主要涉及胆汁盐的疏水侧。在存在光黄素染料的情况下，Tyr-I和Tyr-II的强光CIDNP效应已经在游离辅脂酶上进行了描述[P. Canioni，P. Cozzone和R. 03 The Dog（1980）111，219-222]在牛磺脱氧胆酸盐或鹅胆胺胶束的存在下被完全抑制，表明由于胆汁盐的保护，芳香族表面残基不再可接近。通过对胶束与辅脂酶结合过程中NMR扰动和光CIDNP效应的pH依赖性研究，证实了（1）疏水芳香结构域直接参与作用;（2）胶束与辅脂酶结合的驱动力本质上是疏水性的。最初，脂质疏水结合位点参与结合牛磺脱氧胆酸盐聚集体的构建，以通过疏水表面相互作用（化学计量复合物）形成混合胶束。在较高的胆汁盐浓度，极性力可能占胶束结构的进一步增长结合辅脂酶。
Porcine pancreatic colipase possesses a particular three‐dimensional surface domain containing six out of the seven aromatic residues of the molecule in a highly hydrophobic environment [P. Canioni and P. Cozzone (1979)Biochimie (Paris) 61, 343–354; J. Wieloch, B. Borgström, K. E. Falk and S. Forsen (1979)Biochemistry, 18, 1622–1628]. The domain corresponds to the 49–57 and 77–86 β‐sheet fragments brought into spatial proximity by protein folding [P. Canioni, P. Cozzone and L. Sarda (1980)Biochim. Biophys. Acta, 621, 29–42]. The identification of this specific domain as being the lipid binding site on colipase is proposed on the basis of the NMR and photochemically induced dynamic nuclear polarization (photo‐CIDNP) studies of the complexes of colipase with organized bile salt micelles.The binding of taurodeoxycholate micelles specifically perturbs the proton NMR ring resonances of Tyr‐I and Tyr‐II (Tyr‐56 and Tyr‐57) and His‐II (His‐86) together with several aliphatic resonances, reflecting the involvement of the hydrophobic aromatic domain in micelle fixation. In the presence of colipase, specific shifts and broadening of the methyl groups at position 18 and 21 of the sterane ring of taurodeoxycholate are observed and suggest that the hydrophobic side of the bile salt is primarily involved. The strong photo‐CIDNP effects of Tyr‐I and Tyr‐II in the presence of lumiflavin dye, which have been described on free colipase [P. Canioni, P. Cozzone and R. Kaptein (1980)FFBS Lett. 111, 219–222] are totally suppressed in the presence of taurodeoxycholate or chenocholamine micelles, indicating that due to the protection by the bile salt, the aromatic surface residues are no longer accessible. The pH dependence of the NMR perturbations and photo‐CIDNP effects observed in the colipase‐micelle complexes confirms that (1) the hydrophobic aromatic domain is directly involved and (2) the driving force of the primary micelle binding is essentially hydrophobic.A general model for micelle binding to colipase is proposed and involves a two‐step mechanism. Initially, the lipid hydrophobic binding site participates in the building of the bound taurodeoxycholate aggregate to form a mixed micelle through hydrophobic surface interactions (stoichiometric complex). At higher bile salt concentrations, polar forces might account for further growth of the micellar structure bound on colipase.
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猪胰辅脂肪酶结构中一个酪氨酸和两个组氨酸残基的核磁共振研究
影响因子：
3.5
作者：
T. Wieloch
通讯作者：
T. Wieloch
猪胰辅脂肪酶 A 的 360 MHz 激光 photo-CIDNP
影响因子：
3.5
作者：
P. Canioni;P. Cozzone;R. Kaptein
通讯作者：
R. Kaptein
DOI：
10.1016/0005-2795(74)90142-1
发表时间：
1974
期刊：
Biochimica et biophysica acta
影响因子：
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作者：
M. Charles;C. Erlanson;J. Bianchetta;J. Joffre;A. Guidoni;M. Rovery
通讯作者：
M. Rovery
猪胰辅脂肪酶的构象动力学：360 MHz 质子核磁共振研究
影响因子：
3.5
作者：
P. Cozzone
通讯作者：
P. Cozzone
DOI：
10.1016/0005-2795(74)90143-3
发表时间：
1974
期刊：
Biochimica et biophysica acta
影响因子：
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作者：
C. Erlanson;M. Charles;M. Astier;P. Desnuelle
通讯作者：
P. Desnuelle