STRUCTURAL-ANALYSIS OF DIFFERENTIATION ANTIGENS MO1 AND MO2 ON HUMAN-MONOCYTES

STRUCTURAL-ANALYSIS OF DIFFERENTIATION ANTIGENS MO1 AND MO2 ON HUMAN-MONOCYTES
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DOI:
10.1089/hyb.1.1982.1.329
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发表时间:
1982-01-01
期刊:
影响因子:
--
通讯作者:
TERHORST, C
TERHORST, C
中科院分区:
其他
文献类型:
--
作者:
TODD, RF;VANAGTHOVEN, A;TERHORST, C

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MOL和Mo2是由人单核细胞表达的膜分化抗原,在MO1的情况下是由粒细胞和空细胞表达的。MO1抗原的表达对完整单核细胞的蛋白水解酶处理具有抵抗力,而Mo2的表达对蛋白酶敏感;在有利于蛋白质合成的条件下,经胰酶处理的单核细胞在培养过程中可再生Mo2抗原活性。进一步的生化分析表明,MO1与一种由94,000和155,000 mW两个亚基组成的糖蛋白有关。Mo2位于一个55,000 mW的糖蛋白上。内标记细胞裂解产物中含有MO1和Mo2结构的免疫沉淀表明这些蛋白质是由人单核细胞合成的。
Mol and Mo2 are membrane differentiation antigens expressed by human monocytes, and in the case of Mo1, by granulocytes and null cells. Mo1 antigen expression is resistant to protease treatment of intact monocytes while Mo2 is protease sensitive; Mo2 antigenic activity is regenerated by trypsin-treated monocytes during culture under conditions that favor protein synthesis. Further biochemical analysis reveals that Mo1 is associated with a glycoprotein consisting of two subunits of 94,000 and 155,000 MW. Mo2 resides on a glycoprotein of 55,000 MW. Immunoprecipitation of Mo1- and Mo2-bearing structures from lysates of internally labeled cells indicates that these proteins are synthesized by human monocytes.