Kjeldsen L, Cowland J B, Johnsen A H, Borregaard N
Granulocyte Research Laboratory, Department of Hematology, The Finsen Center, Rigshospitalet, Denmark.
FEBS Lett. 1996 Feb 19;380(3):246-50. doi: 10.1016/0014-5793(96)00030-0.
A novel 28 kDa glycoprotein was purified from exocytosed material from human neutrophils and its primary structure partially determined. Degenerate oligonucleotide primers were used to amplify cDNA clones from a human bone marrow cDNA library. The deduced 245 amino acid sequence of the 2124 bp full-length cDNA showed high degrees of similarity to the deduced sequences of human gene TPX-1 and of sperm-coating glycoprotein from rat and mouse. Subcellular fractionation of human neutrophils indicated that the protein is localized in specific granules. The protein was named SGP28 (specific granule protein of 28 kDa).
从人中性粒细胞胞吐物质中纯化出一种新型的28 kDa糖蛋白,并部分确定了其一级结构。使用简并寡核苷酸引物从人骨髓cDNA文库中扩增cDNA克隆。2124 bp全长cDNA推导的245个氨基酸序列与人类基因TPX-1以及大鼠和小鼠精子包被糖蛋白的推导序列高度相似。人中性粒细胞的亚细胞分级分离表明该蛋白定位于特定颗粒中。该蛋白被命名为SGP28(28 kDa特异性颗粒蛋白)。