Analysis of the aliphatic 1H-NMR spectrum of plasminogen kringle 4. A comparative study of human, porcine, bovine and chicken homologs.
Analysis of the aliphatic 1H-NMR spectrum of plasminogen kringle 4. A comparative study of human, porcine, bovine and chicken homologs.
复制标题
纤溶酶原三环的脂肪族1H-NMR谱分析。人、猪、牛和鸡同系物的比较研究。
DOI：
10.1111/j.1432-1033.1988.tb13734.x
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发表时间：
1988
期刊：
影响因子：
--
通讯作者：
Llinás,M
中科院分区：
文献类型：
--
作者：
Petros,AM;Gyenes,M;Patthy,L;Llinás,M
通过二维化学位移关联(COSY)和核Overhauser关联(NOESY)实验，研究了人纤溶酶原kringle4结构域在300 MHz和620 MHz下的脂肪族~1H-核磁共振波谱。已经确定了一些脂肪族质子自旋系统，并进行了几个明确的指认。这主要是通过将人的kringle4与猪、牛和鸡的同源物的谱进行比较，以及与我们先前报道的人纤溶酶原kringle1的谱进行比较来实现的。人kringle4的三个丙酮基和两个亮氨基残基已被指认。通过接力COSY实验确定了11个苏酮基自旋系统，并对Thr17进行了归属。三个丙氨基自旋系统已被确认和指认。已鉴定了6个丝氨基自旋系统，并定位了来自人kringle4的7个甘氨基残基的信号，并指定了Gly45。此外，在人的Kringle4的COSY谱中绘制了24个AMX自旋系统，并归属了Tyr2、Tyr41、Tyr50、Tyr74、Trp25和Trp62的Hα-Hβ，β自旋系统。从一个去糖化的鸡同系物的光谱中，归属了Met28和Met48的ɛ-甲基单线团。最后，观察到配体对所选择的脂肪族共振的影响，这可以根据kringle赖氨酸结合位点附近的残基来分析。
The aliphatic1H‐NMR spectrum of the kringle 4 domain of human plasminogen has been studied via two‐dimensional chemical shift correlated (COSY) and nuclear Overhauser correlated (NOESY) experiments at 300 MHz and 620 MHz. A number of aliphatic proton spin systems have been identified and several definite assignments have been made. This was mainly achieved by comparison of the human kringle 4 spectrum with spectra of the porcine, bovine and chicken homologs and also with that of the kringle 1 from human plasminogen on which we have reported previously. The three valyl and two leucyl residues of human kringle 4 have been assigned. The eleven threonyl spin systems have been identified via a RELAYED‐COSY experiment and Thr17has been assigned. The three alanyl spin systems have been identified and assigned. Six seryl spin systems have been identified and the signals from the seven glycyl residues of human kringle 4 have been located with Gly45assigned. Furthermore, 24 AMX spin systems have been mapped in the COSY spectrum of human kringle 4 and Hα‐Hβ,β′spin systems of Tyr2, Tyr41, Tyr50, Tyr74, Trp25and Trp62have been assigned. From the spectrum of a deglycosylated chicken homolog, the ɛ‐methyl singlets of Met28and Met48have been assigned. Finally, ligand effects on selected aliphatic resonances were observed which could be analyzed in terms of residues likely to neighbor the kringle lysine‐binding site.