Summary
Active kallikreins isolated from various exocrine and endocrine tissues were identified by a monoclonal antibody in Western blot analyses to be ~ 38,000 dalton proteins. Kallikreins isolated from rat pancreas, kidney, submandibular gland, brain, spleen and urine were indistinguishable with respect to molecular weight and immunological characteristics. Preprokallikreins were synthesized in a cell-free translation system directed by mRNAs and immunoprecipitated by affinity-purified kallikrein antibody. Analysis of the precipitates by SDS-polyacrylamide gel electrophoresis revealed a ~ 37,000 dalton polypeptide in kidney, brain and submandibular gland translation products. This 37,000 dalton kallikrein precursor was hybrid- arrested by a kallikrein cDNA encoding tissue kallikrein which was isolated from a rat submandibular gland cDNA library. The immunoprecipitates of products directed by pancreaticv mRNA showed a major protein with Mr of ~ 30,000. An endogenous ~ 92,000 dalton component in rat urine and kidney was also identified by a monoclonal antibody to tissue kallikrein and represents a kallikrein-inhibitor complex. These results indicate that tissue kallikreins can be initially synthesized as 37,000 or 30,000 dalton prepropeptides and then converted into a 38,000 dalton active form by proteolytic processing and glycosylation. The active kallikrein is capable of binding to an inhibitor to form a 92,000 dalton complex.
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© 1986 Plenum Press, New York
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Chao, J., Chao, L., Woodley, C.M., Gerald, W., Margolius, H.S. (1986). Active Kallikrein, Preprokallikrein, and Kallikrein-Inhibitor Complex. In: Greenbaum, L.M., Margolius, H.S. (eds) Kinins IV. Advances in Experimental Medicine and Biology, vol 198A. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5143-6_25
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DOI: https://doi.org/10.1007/978-1-4684-5143-6_25
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