淡水蟹帕拉塞尔福斯水栖蟹（赫布斯特）血清中一种天然血凝素的特性分析。

Characterization of a natural hemagglutinin in the serum of a freshwater crab Parathelphusa hydrodromus (Herbst).

作者信息

Nalini M, Mullainadhan P, Arumugam M

机构信息

Department of Zoology, University of Madras, India.

出版信息

Arch Int Physiol Biochim Biophys. 1994 Sep-Oct;102(5):259-64. doi: 10.3109/13813459409003941.

DOI:10.3109/13813459409003941

PMID:7849273

Abstract

A naturally occurring hemagglutinin (HA) was detected in the serum of the freshwater crab Parathelphusa hydrodromus using mammalian erythrocytes (RBC) as indicator cells. The serum gave the highest HA titer with rabbit RBC. In cross adsorption tests, this RBC type completely adsorbed all HA activities from serum. An analysis of the physico-chemical properties of HA showed it to be specifically dependent on the presence of Ca2+ for its activity, irreversibly sensitive to EDTA, stable between pH 7.5 and 10.0, and heat-labile. Further studies demonstrated that the HA is proteinaceous as it was precipitable by conventional deproteinizing agents, and susceptible to the action of proteases and 2-mercaptoethanol. HA-inhibition assays performed with 44 carbohydrates revealed that the serum HA was specific for non-reducing terminal glucose with alpha 1-2 glycosidic linkage. Thus this agglutinin appears to be unique among all the known crustacean agglutinins.

摘要

使用哺乳动物红细胞（RBC）作为指示细胞，在淡水蟹Parathelphusa hydrodromus的血清中检测到一种天然存在的血凝素（HA）。该血清对兔红细胞的血凝效价最高。在交叉吸附试验中，这种红细胞类型完全吸附了血清中的所有HA活性。对HA理化性质的分析表明，其活性特别依赖于Ca2+的存在，对EDTA不可逆敏感，在pH 7.5至10.0之间稳定，且对热不稳定。进一步研究表明，HA是蛋白质，因为它可被传统的脱蛋白剂沉淀，并且易受蛋白酶和2-巯基乙醇的作用影响。用44种碳水化合物进行的HA抑制试验表明，血清HA对具有α 1-2糖苷键的非还原末端葡萄糖具有特异性。因此，这种凝集素在所有已知的甲壳类凝集素中似乎是独特的。