Abstract
Rabbit prekallikrein (RPK) was purified from rabbit plasma by ion exchange and lectin column chromatography and preparative polyacrylamide gel electrophoresis. A 1500-fold purification was routinely achieved with a final yield of 5–10%, The purified RPK was found to be a glycoprotein with an apparent molecular weight of 88,000. Activation of RPK with either trypsin or rabbit Hageman factor (active) occurs by limited proteolytic cleavage, producing two disulfide-linked polypeptide chains with molecular weights of 55,000 and 35,000. Both chains contain carbohydrate and the 35,000-molecular-weight polypeptide was shown to incorporate [3H]DFP. Activation of RPK in kaolin-treated plasma was shown to proceed by an analogous mechanism yielding 55,000- and 35,000-molecular-weight polypeptide chains.
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This work was supported by United States Public Health Service Grant AI-07007 and HL-16411.
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Ulevitch, R.J., Cochrane, C.G. & Johnston, A.R. Rabbit prekallikrein. Inflammation 4, 9–25 (1980). https://doi.org/10.1007/BF00914099
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DOI: https://doi.org/10.1007/BF00914099