胰蛋白酶有限蛋白水解对人触珠蛋白的影响

Iwona Katnik, Wanda Dobryszycka
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引用次数: 3

摘要

胰蛋白酶消化触珠蛋白产生四种糖肽。在2-巯基乙醇存在或不存在的情况下,通过薄层色谱和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定了糖肽的氨基酸组成和分子量。研究了血红蛋白结合能力和免疫特性。糖肽I和II不与血红蛋白形成活性复合物,对接触珠蛋白与特异性抗血清的反应抑制作用达70%以上。糖肽III和IV分别具有11%和4%的血红蛋白结合能力和82%和67%的抗原反应性。糖肽IV含有三个抗原决定因子,而糖肽III含有四个,其中一个被胰蛋白酶消化暴露。在交叉双向免疫电泳中,糖肽III显示出至少4种成分与抗触珠蛋白血清反应,糖肽IV显示出2种成分。
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The effects of limited proteolysis by trypsin on human haptoglobin

Trypsin digestion of haptoglobin resulted in four glycopeptides. The glycopeptides were characterized by amino acid composition and molecular weight, as determined by thin-layer chromatography, and sodium dodecyl sulphate-polyacrylamide gel electrophoresis in the presence or absence of 2-mercaptoethanol. Hemoglobin-binding capacity and immunological properties were investigated. Glycopeptides I and II did not form an active complex with hemoglobin and they inhibited the reaction of haptoglobin with specific antiserum by over 70%. Glycopeptides III and IV showed 11 and 4% of the hemoglobin-binding capacity and 82 and 67% of antigenic reactivity of native haptoglobin, respectively. Glycopeptide IV contained three antigenic determinants, whereas glycopeptides III contained four, one of them being exposed by trypsin digestion. In crossed two-dimensional immunoelectrophoresis, glycopeptide III showed at least four components reacting with antihaptoglobin serum, and glycopeptide IV, two components.

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