AUTOROSETTE INHIBITION-FACTOR - ISOLATION AND PROPERTIES OF THE HUMAN-PLASMA PROTEIN
AUTOROSETTE INHIBITION-FACTOR - ISOLATION AND PROPERTIES OF THE HUMAN-PLASMA PROTEIN
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DOI：
10.1111/j.1432-1033.1981.tb05655.x
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发表时间：
1981-01-01
期刊：
影响因子：
--
通讯作者：
PARISH, CR
中科院分区：
文献类型：
--
作者：
RYLATT, DB;SIA, DY;PARISH, CR
The sera of many vertebrates, including man, contain a factor, termed autorosette inhibition factor, which can inhibit the ability of murine lymphocytes to bind autologous erythrocytes. Utilizing the strong affinity of this inhibitor for phosphocellulose, a 1-column procedure was developed for the isolation of autorosette inhibition factor which gives a 1000-fold purification with 85% recovery of biological activity. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and gel filtration of the purified protein gave apparent MW of 80,000. The glycoprotein appears to be present in serum at levels of 5-20 mg/100 ml (.apprx. 1 .mu.M) and can completely block murine autorosetting at concentrations of 50 nM. Amino acid analysis of human autorosette inhibition factor suggested that this protein might be closely related to the previously described lower MW, histidine-rich glycoprotein and plasminogen-binding protein in human plasma. In support of this notion was the observation that purified human autorosette inhibition factor cross-reacted strongly with a monospecific antiserum to histidine-rich glycoprotein; this antiserum also neutralized the biological activity of autorosette inhibition factor. These results are consistent with autorosette inhibition factor being a larger MW precursor from which histidine-rich glycoprotein and, possibly, plasminogen-binding protein are derived by proteolysis during purification.
