Sugiyama K, Ogino T, Ogata K
Department of Pharmacology, Okayama University Dental School, Japan.
Jpn J Pharmacol. 1989 Feb;49(2):165-71. doi: 10.1254/jjp.49.165.
Treatment of human serum albumin with a proteolytic enzyme such as pepsin, alpha-chymotrypsin, cathepsin D or trypsin generated histamine releasing peptides. A low-molecular weight peptide (P-1) responsible for releasing histamine was isolated from peptic digests of human serum albumin by affinity chromatography on heparin-Ultrogel and reversed-phase high performance liquid chromatography. The amino acid sequence of the P-1 was estimated to be V-R-Y-T-K-K-V-P-Q-V-S-T-P-T-L by Edman degradation. The sequence determined appears to correspond to residues 409-423 of human serum albumin. Peptide P-1 produced dose-related histamine release from isolated rat mast cells in the concentration range of 1-50 microM. The intradermal injection of the P-1 (0.5 micrograms) increased capillary permeability in rats. This response was blocked by the antihistamine diphenhydramine.
用人血清白蛋白与诸如胃蛋白酶、α-胰凝乳蛋白酶、组织蛋白酶D或胰蛋白酶等蛋白水解酶处理可产生组胺释放肽。通过肝素琼脂糖凝胶亲和色谱和反相高效液相色谱，从人血清白蛋白的胃蛋白酶消化物中分离出一种负责释放组胺的低分子量肽（P-1）。通过埃德曼降解法估计P-1的氨基酸序列为V-R-Y-T-K-K-V-P-Q-V-S-T-P-T-L。所确定的序列似乎与人血清白蛋白的409-423位残基相对应。肽P-1在1-50微摩尔的浓度范围内，从分离的大鼠肥大细胞中产生了剂量相关的组胺释放。皮内注射P-1（0.5微克）可增加大鼠的毛细血管通透性。这种反应被抗组胺药苯海拉明阻断。
