THE C-TERMINAL HALF OF THE PORCINE ESTRADIOL-RECEPTOR CONTAINS NO POSTTRANSLATIONAL MODIFICATION - DETERMINATION OF THE PRIMARY STRUCTURE
THE C-TERMINAL HALF OF THE PORCINE ESTRADIOL-RECEPTOR CONTAINS NO POSTTRANSLATIONAL MODIFICATION - DETERMINATION OF THE PRIMARY STRUCTURE
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DOI：
10.1016/0303-7207(94)90119-8
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发表时间：
1994-09-01
影响因子：
4.1
通讯作者：
THOLE, HH
中科院分区：
文献类型：
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作者：
BOKENKAMP, D;JUNGBLUT, PW;THOLE, HH
猪雌二醇受体从H-267延伸到I-595，通过吸附在单抗13H2上，在天然和变性状态下都能被CNBr、邻碘苯甲酸和内肽酶Lys-C等酶所切割。反相高效液相色谱分离，Edman降解测序，E区缺少T-570-M(581)。未发现翻译后修饰的证据；天然片段没有糖基化，E区(AA 328,331,459,526,537)和F(AA 582,583)的酪氨酸残基没有磷酸化。此外，所有的丝氨酸和苏氨酸PTH衍生物都以正常的产率得到。该片段的氨基酸序列与来源于该基因的氨基酸序列完全一致。该全序列编码595个氨基酸的多肽，计算质量为66357Da。猪受体在C和E结构域的物种之间具有高度的同源性。
The C-terminal part of ligand filled porcine estradiol receptor extending from H-267 to I-595 was isolated by adsorption to the monoclonal antibody 13H2, subjected to cleavage by CNBr, o-iodosobenzoic acid and endopeptidase Lys-C as well as other proteases, both in the native and the denatured state. The overlapping peptides produced were separated by reverse phase HPLC and sequenced by Edman degradation, lacking T-570-M(581) in domain E We found no evidence of post-translational modification; the native fragment is not glycosylated and the tyrosyl residues in domain E (aa 328, 331, 459, 526, 537) and F (aa 582, 583) are not phosphorylated. In addition, all serine and threonine PTH derivatives were obtained in normal yields. The amino acid sequence of the fragment corresponds in full with that derived from the cDNA. The complete cDNA-derived sequence codes for a polypeptide of 595 amino acids with a calculated mass of 66 357 Da. The high degree of homology between species in domains C and E is shared by the porcine receptor.