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- W2081897910 abstract "A method is described for the isolation of lysozyme from human placenta. The procedure utilizes an initial separation of lysozyme from mucoproteins and globulins, as well as contaminating hemoproteins, in placenta, the subsequent batchwise fractionation on CM-Sephadex, and a final chromatographic purification on CM-cellulose and on Sephadex G-100. The isolated enzyme showed a purification of 1550-fold on the basis of the initial fraction precipitated with ammonium sulfate, and had a specific activity of 3.2 in comparison with 1.0 for egg-white lysozyme. Cellulose acetate electrophoresis and sedimentation behavior of the enzyme preparation indicated it to be homogeneous. The enzyme seemed to have an isoelectric point of pH 11.7 and apparently possessed a low molecular weight since the sedimentation coefficient (s20, w) was 1.8S. The enzyme was found to be labile at alkaline pH." @default.
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- W2081897910 date "1971-08-01" @default.
- W2081897910 modified "2023-10-16" @default.
- W2081897910 title "Method for isolation of human placental lysozyme" @default.
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- W2081897910 doi "https://doi.org/10.1016/0003-2697(71)90042-x" @default.
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