Abstract
Hemolytical serum or crude homogenates of red blood cells have long been known to inactivate or degrade insulin [1–4]. When a possible effect of insulin on red cell metabolism was investigated, this very fact occurred to us as a troublesome problem [5]. The half-life of the turnover of the insulin molecule in the human system has been found to be about 12–40 min. The degradation of insulin has been attributed to two different pathways: a) reductive cleavage of the disulfide bridges by means of an enzyme (glutathione-insulin-transhydrogenase) [6–15], and b) proteolytic degradation by an insulin-specific proteinase [16–22].
Supported by the Deutsche Forschungsgemeinschaft.
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Tschesche, H., Dietl, T., Kolb, H.J., Standl, E. (1974). An Insulin Degrading Proteinase from Human Erythrocytes and Its Inhibition by Proteinase Inhibitors. In: Fritz, H., Tschesche, H., Greene, L.J., Truscheit, E. (eds) Proteinase Inhibitors. Bayer-Symposium, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-87966-1_65
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