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- W1983573889 abstract "Abstract 1. 1. Trypsin inhibitors in serum from adult and suckling rats and in rat milk were studied by gel filtration and electrophoresis in casein-agarose gels. In addition trypsin binding properties and inhibiting activity in the presence of low mol. wt substrates were studied. 2. 2. In adult rat serum 6 trypsin inhibitors were found, most of these having not been described before. One inhibitor, di-macroglobulin is a homologue of human α2-macroglobulin. Two inhibitors in the α1- and α2-regions of the electropherogram had a mol. wt of about 200,000. The third group of inhibitors was eluted together with albumin and had electrophoretic mobilities in the di-α2- and β-region. 3. 3. In the serum of the newborn rat the inhibitors of the third protein peak dominated, especially that in the α2-region. In later developmental stages the inhibitor pattern became increasingly similar to that of the adult. A specific inhibitor, α2-acute phase globulin, was found in the neonatal rat but disappeared in later developmental stages. 4. 4. The trypsin inhibitors in rat milk were dominated by inhibitors in the third protein peak after gel nitration and had the same electrophoretic mobilities as the inhibitors of the corresponding fraction in serum. No low mol. wt trypsin inhibitors specific for milk were found. 5. 5. Rat milk trypsin inhibiting activity seems to have a higher resistance to low pH-values than the inhibiting activity of rat serum. 6. 6. The trypsin inhibitor pattern in the serum of the suckling rat is similar to that of milk, indicating an absorption of inhibitors from milk. The milk inhibitors may have the function of preventing protein breakdown in the intestine of the suckling rat." @default.
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- W1983573889 date "1976-01-01" @default.
- W1983573889 modified "2023-10-17" @default.
- W1983573889 title "Trypsin inhibitors in serum of adult and suckling rats and in rat milk" @default.
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- W1983573889 doi "https://doi.org/10.1016/0020-711x(76)90036-7" @default.
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