Calvete J J, Costa F H, Saker-Sampaio S, Murciano M P, Nagano C S, Cavada B S, Grangeiro T B, Ramos M V, Bloch C, Silveira S B, Freitas B T, Sampaio A H
Instituto de Biomedicina de Valencia, Spain.
Cell Mol Life Sci. 2000 Feb;57(2):343-50. doi: 10.1007/PL00000696.
The primary structure of a lectin isolated from the red alga Bryothamnion triquetrum was established by combination of Edman degradation of sets of overlapping peptides and mass spectrometry. It contains 91 amino acids and two disulphide bonds. The primary structure of the B. triquetrum lectin does not show amino acid sequence similarity with known plant and animal lectin structures. Hence, this protein may be the paradigm of a novel lectin family.
通过对重叠肽段进行埃德曼降解并结合质谱分析,确定了从红藻三楞叶藓(Bryothamnion triquetrum)中分离出的一种凝集素的一级结构。它含有91个氨基酸和两个二硫键。三楞叶藓凝集素的一级结构与已知的植物和动物凝集素结构没有氨基酸序列相似性。因此,这种蛋白质可能是一个新型凝集素家族的范例。