By Silvio Garattini and Parkhurst A. Shore (Eds.)
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19631)). The use of synthetic bradykinin and kallidin instead of the crude material was not the answer to all the problems. Dilute solutions of the peptitles are quite unstable. This instability is caused at least in part by losing the active material by adsorption on glass. Various techniques are recommended for avoiding this apparent decrease of activity. , 1965) could be helpful in preventing the loss of material. Commercial preparations of bradykinin may contain chlorobutanol as a preservative (Collier, 1965).
Kinins had been prepared (Schrodcr and Hempel, 1964), but only a limited * See note added in proof a t the end of this chapter. 22 ERVIN G . ERDOS number of conclusions could be drawn from these studies. , 1961). The analogs of these peptides have been studied more extensively because they have been available for a longer period and more specific assay systems have been developed for them than for bradykinin. , 1964; Schroder and Lubke, 1964) remain biologically effective, but only the longer analogs of bradykinin are active.
CM-cellulose chromatography at 4" of the product from second Sephadex chromatogram. 0. 67 x 23 em. 5. Volume of mixing chamber: 125 ml. Fraction volume: 2 ml (Pierce and Webster, 1961). et al. released kallidin from bovine plasina with subinaxillary kallikrein. The former authors obtained a significant aiiiouiit of bradykinin in addition to kallidin, but this niight have been due l o the acidification of plasma. Werle et al. (1961) found only 10% bradykinin after purifying kallidin. The purification procedure of Pierce and Webster consisted of the sequential use of adsorption on Amberlite XE-64 ion exchange resin, Sephadex filtration, and CM-cellulose chroniatography (see Fig.
Advances in Pharmacology by Silvio Garattini and Parkhurst A. Shore (Eds.)