Abstract
Publisher Summary This chapter presents the procedure for purification and assaying of kininogens. In general, purification of LMW kininogen requires many steps and the recovery from plasma is very low. Steps of purification include ion-exchange column chromatography on DEAE-Sephadex or QAE-Sephadex, CM-Sephadex or SP-Sephadex and gel filtration. However, a difficulty in the purification of HMW kininogen is the susceptibility of the kininogen to plasma kallikrein. Kininogen can be estimated by measuring kinin biologically or immunologically following incubation with kinin-releasing enzymes. Differential assay for HMW kininogen and LMW kininogen is obtained by utilizing the specificity of kinin-releasing enzymes. Plasma kallikrein liberates bradykinin from HMW kininogen, whereas glandular kallikrein liberates kallidin from both of high molecular weight and low molecular weight kininogens. Trypsin and snake venom kininogenase liberate bradykinin from both kininogens. For the bioassay of kininogens, attention should be paid to the contamination of kininase or inhibitors for enzymes in kininogen preparation, especially when partially purified kininogen or plasma is used.
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