关于人降钙素M的免疫化学研究，以获取有关分子形状的信息。
Immunochemical studies on human calcitonin M leading to information on the shape of the molecule.
作者信息
Byfield P G, Clark M B, Turner K, Foster G V, MacIntyre I
出版信息
Biochem J. 1972 Mar;127(1):199-206. doi: 10.1042/bj1270199.
Abstract
- Two antisera were obtained from a single rabbit. Both are highly specific for human calcitonin M but react with different parts of the amino acid sequence. 2. The different sequences that react with the antibodies of the two antisera were located. The first antiserum reacts at two sites in the molecule, one in the sequence residues 11-18, probably with residue 17 as the immunodominant group, and another on either side of the 28-29 peptide bond. The second antiserum, harvested 9 months later, reacts principally at one site bridging the 28-29 peptide bond. 3. A consideration of the properties of the hormone's binding sites and of data relating biological activity to structure enables some conclusions to be drawn with regard to the shape of the molecule. It appears that the peptide chain is folded to bring N- and C-termini closer together and that there is non-covalent interaction between regions in the chain near both termini. One of these is located near residue 8.
摘要
- 从一只兔子身上获得了两种抗血清。两者对人降钙素M都具有高度特异性，但与氨基酸序列的不同部分发生反应。2. 确定了与两种抗血清抗体发生反应的不同序列。第一种抗血清在分子中的两个位点发生反应，一个在序列残基11 - 18处，可能以残基17作为免疫显性基团，另一个在28 - 29肽键的两侧。9个月后采集的第二种抗血清主要在跨越28 - 29肽键的一个位点发生反应。3. 考虑激素结合位点的性质以及将生物活性与结构相关联的数据，能够就分子的形状得出一些结论。似乎肽链折叠使得N端和C端靠得更近，并且在链中靠近两个末端的区域之间存在非共价相互作用。其中一个位于残基8附近。
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