Ohkubo I, Niwa M, Sasaki M
Department of Biochemistry, Nagoya City University Medical School, Japan.
Prep Biochem. 1988;18(4):413-30. doi: 10.1080/00327488808062541.
Zn-alpha 2-glycoprotein (Zn alpha 2gp) was purified from fresh human plasma approximately 670-fold in a yield of 18% over the fractions from DEAE-Sephadex A-50 column chromatography. The purified protein was a glycoprotein with molecular weights of 56,000 and 57,000 on Superose and Sephadex G-150 column chromatographies and of 41,000 and 42,000 on nonreduced SDS-PAGE. Characterization, which included a determination of molecular weight, amino acid composition, amino terminus, and antigenicity, correlated well with known values previously reported for human Zn alpha 2gp.
从新鲜人血浆中纯化出锌α2-糖蛋白(Znα2gp),经DEAE-葡聚糖A-50柱层析,纯化倍数约为670倍,产率为18%。纯化后的蛋白质是一种糖蛋白,在Superose和Sephadex G-150柱层析上分子量为56,000和57,000,在非还原SDS-PAGE上分子量为41,000和42,000。包括分子量测定、氨基酸组成、氨基末端和抗原性测定在内的表征结果与先前报道的人Znα2gp已知值高度相关。