Wang R, Liang Z, Hal M, Söderhall K
Department of Comparative Physiology, Evolutionary Biology Centre, Uppsala University, Sweden.
Fish Shellfish Immunol. 2001 Oct;11(7):623-37. doi: 10.1006/fsim.2001.0341.
The crayfish haemolymph can form stable and insoluble clots by a transglutaminase (TGase)-catalysed crosslinking reaction between the soluble clotting protein molecules from the plasma. The crayfish haemocytes, both semigranular and granular cells, as well as the muscle tissue, contain TGase activity, whereas the hepatopancreas and plasma have no TGase activity. A 3199 bp cDNA encoding a TGase was isolated from a crayfish haemocyte cDNA library. The deduced protein comprises 766 amino acid residues and has a calculated molecular mass of between 85,930 and 86,034 kDa due to four amino acid variations. This gene is expressed as a single 4.9 kb transcript exclusively in the haemocytes and at very low levels in muscle and the hepatopancreas. Sequence comparison shows that this TGase has significant similarities to other TGases from invertebrates and mammals.
小龙虾血淋巴可通过转谷氨酰胺酶(TGase)催化血浆中可溶性凝血蛋白分子之间的交联反应形成稳定且不溶性的凝块。小龙虾血细胞,包括半颗粒细胞和颗粒细胞,以及肌肉组织,都含有TGase活性,而肝胰腺和血浆则没有TGase活性。从小龙虾血细胞cDNA文库中分离出一个编码TGase的3199 bp cDNA。推导的蛋白质包含766个氨基酸残基,由于四个氨基酸变异,计算分子量在85930至86034 kDa之间。该基因仅在血细胞中以单一4.9 kb转录本形式表达,在肌肉和肝胰腺中的表达水平非常低。序列比较表明,这种TGase与来自无脊椎动物和哺乳动物的其他TGase有显著相似性。