Hough D W, McIlroy B M, Stevenson G T
Immunology. 1977 Mar;32(3):337-43.
Limited proteolysis of lymphocytic surface immunoglobulins in guinea-pig, rabbit and man was investigated by immunofluorescence using conjugated antisera specific for immunoglobulin fragments. The cell surface IgM of guinea pig L2C leukaemic lymphocytes and rabbit blood lymphocytes was cleaved in situ at its hinge region by papain. The Fcmicron fragment remained attached to the membrane and could be stained with the appropriate anti-Fc conjugate. The surface IgD and IgM of human chronic lymphocytic leukaemia cells was cleared from the cell surface by papain, as shown by reagents directed against both Fab and Fc region determinants. This could be due either to proteolytic degradation of membrane bound Fc or to initial cleavage of Ig from the membrane at some point other than the hinge region.
利用针对免疫球蛋白片段的共轭抗血清，通过免疫荧光法研究了豚鼠、兔子和人类淋巴细胞表面免疫球蛋白的有限蛋白水解。豚鼠L2C白血病淋巴细胞和兔子血液淋巴细胞的细胞表面IgM在其铰链区被木瓜蛋白酶原位切割。Fcmicron片段仍附着在膜上，可用适当的抗Fc共轭物染色。针对Fab和Fc区域决定簇的试剂显示，木瓜蛋白酶可将人类慢性淋巴细胞白血病细胞表面的IgD和IgM清除。这可能是由于膜结合Fc的蛋白水解降解，或者是由于Ig在铰链区以外的某个点从膜上最初被切割。
