Chadli A, LeCaer J P, Bladier D, Joubert-Caron R, Caron M
Laboratoire de Biochimie et Technologie des Protéines, Université Paris-Nord, Bobigny, France.
J Neurochem. 1997 Apr;68(4):1640-7. doi: 10.1046/j.1471-4159.1997.68041640.x.
Our previous studies have characterized an endogenous lectin from human brain identified as galectin-1. A soluble ligand of galectin-1 was purified from human brain by affinity chromatography and preparative electrophoresis. The purified ligand (termed HBGp82, for human brain galectin-1-binding polypeptide of 82,000 daltons) has an apparent molecular mass of 82 kDa and is glycosylated by N-linked biantennary complex structures. HBGp82 was partially characterized by microsequencing of peptide fragments. Similar peptides were found in a heat shock of protein of 90,000 daltons, hsp90. However, comparison of apparent molecular weights and matrix-assisted laser desorption mass spectrometry clearly showed that HBGp82 differs to some degree from hsp90.
我们之前的研究已对一种源自人脑的内源性凝集素（鉴定为半乳糖凝集素-1）进行了表征。通过亲和色谱法和制备电泳从人脑中纯化出了半乳糖凝集素-1的一种可溶性配体。纯化后的配体（称为HBGp82，即82,000道尔顿的人脑半乳糖凝集素-1结合多肽）的表观分子量为82 kDa，且通过N-连接的双天线复合结构进行糖基化。通过对肽片段进行微量测序对HBGp82进行了部分表征。在90,000道尔顿的热休克蛋白hsp90中发现了类似的肽段。然而，表观分子量的比较以及基质辅助激光解吸质谱分析清楚地表明，HBGp82在一定程度上与hsp90不同。
