Identification of gastrin releasing peptide-related substances in guinea pig and rat brain.
Identification of gastrin releasing peptide-related substances in guinea pig and rat brain.
复制标题
豚鼠和大鼠脑中胃泌素释放肽相关物质的鉴定。
DOI：
10.1016/0006-291x(83)91497-3
复制
发表时间：
1983
影响因子：
3.1
通讯作者：
Chang,JK
中科院分区：
文献类型：
--
作者：
Roth,KA;Evans,CJ;Lorenz,RG;Weber,E;Barchas,JD;Chang,JK
通过与凝胶过滤和反相高效液相色谱（RP-HPLC）连接的序列特异性放射免疫测定法，检查大鼠和豚鼠脑提取物中胃泌素释放肽（GRP）样物质的发生情况。胰蛋白酶消化的免疫反应性肽，然后通过RP-HPLC用于进一步表征脑中的GRP相关肽。使用这些分析技术，发现豚鼠脑提取物含有与真实GRP（27个氨基酸残基长）特征相同的肽。在豚鼠脑提取物中还存在具有GRP特征的羧基末端片段（18-27）以及具有GRP特征的相应氨基末端片段（1-16）。GRP（18-27）似乎与之前在哺乳动物脑提取物中描述的铃蟾肽相关物质相对应。大鼠脑提取物还含有具有GRP（18-27）特征的肽。然而，相应的氨基末端片段在RP-HPLC上的表现与真实GRP（1-16）不同，并且其不被针对真实GRP的氨基末端十三肽片段的抗体识别。类似地，来自大鼠脑的GRP样肽在RP-HPLC上不与真实的GRP共迁移，并且不与针对GRP的氨基末端的抗体反应。
Rat and guinea pig brain extracts were examined for the occurrence of gastrin-releasing peptide (GRP)-like substances by sequence specific radioimmunoassays interfaced with gel filtration and reversed phase high performance liquid chromatography (RP-HPLC). Tryptic digestion of the immunoreactive peptides followed by RP-HPLC was used to further characterize GRP-related peptides in brain. Using these analytical techniques it was found that guinea pig brain extracts contained a peptide with characteristics identical to authentic GRP (27 amino acid residues long). A carboxyterminal fragment with the characteristics of GRP(18–27) as well as a respective aminoterminal fragment with the characteristics of GRP(1–16) were also present in guinea pig brain extracts. The GRP(18–27) seems to correspond to the bombesin related material that has been described previously in mammalian brain extracts.Rat brain extracts also contained a peptide with the characteristics of GRP(18–27). The corresponding aminoterminal fragment, however, behaved differently on RP-HPLC from authentic GRP(1–16) and it was not recognized by antibodies directed to the aminoterminal tridecapeptide fragment of authentic GRP. Similarly the GRP-like peptide from rat brain did not comigrate on RP-HPLC with authentic GRP and was unreactive to antibodies directed toward the aminoterminus of GRP.