Brock J H, Arzabe R, Piñeiro A, Olivito A M
Immunology. 1977 Feb;32(2):207-13.
Digestion of bovine colostral whey with trypsin or chymotrypsin caused a progressive loss of the complement-mediated bactericidal activity of naturally-occurring colostral antibodies of E. coli 0111. Bactericidal activity was associated primarily with IgG1 immunoglobulin and to a lesser extent with IgM. Chymotrypsin preferentially attacked IgM, destroying its antibacterial activity and producing an apparent decrease in its mol wt. Trypsin preferentially attacked IgG1, but loss of antibacterial activity was in this case not accompanied by a decrease in molecular weight. Using colostral whey with antiperoxidase activity it was shown that the kinetics of loss of specific antibody activity were similar to those of loss of bactericidal activity. It is therefore suggested that trypsin may cause a loss of specific antibody activity of colostral IgG1 without cleaving the immunoglobulin molecule.
用胰蛋白酶或糜蛋白酶消化牛初乳乳清会导致大肠杆菌0111天然存在的初乳抗体的补体介导杀菌活性逐渐丧失。杀菌活性主要与IgG1免疫球蛋白相关,与IgM的相关性较小。糜蛋白酶优先攻击IgM,破坏其抗菌活性并使其分子量明显降低。胰蛋白酶优先攻击IgG1,但在这种情况下,抗菌活性的丧失并未伴随着分子量的降低。使用具有抗过氧化物酶活性的初乳乳清表明,特异性抗体活性丧失的动力学与杀菌活性丧失的动力学相似。因此,有人提出胰蛋白酶可能导致初乳IgG1的特异性抗体活性丧失,而不会裂解免疫球蛋白分子。