Guinea Pig Prekallikrein Activator

Treloar, Mary P.; Pyle, Helen A.; Fuller, Penelope J.; Movat, Henry Z.

doi:10.1007/978-1-4684-7439-8_8

Cited by 3 publications

(4 citation statements)

References 7 publications

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“…Although it appears very likely that the PKA obtained in this study is identical to that obtained from whole serum [7], this, too, could be solved only with certainty with the aid of a specific antibody.…”

Section: Discussionmentioning

confidence: 87%

“…[35] or the a,-macroglobulin which complexes with kallikrein [ 3 6 ] and probably with PKA [7]. Natural inhibitors of kinin have also been demonstrated [37].…”

Section: Discussionmentioning

confidence: 98%

“…From whole serum some of the activator was recovered as a small molecular weight (< 40 000), highly anionic substance, which activated prekallikrein. However, the bulk of the prekallikrein activator (PKA) in whole serum was recovered from the macroglobulin fraction, During chromatography a gradual fragmentation occurred, until most of the material had a molecular weight of less than 40 000, similar t o the PKA recovered initially from the whole serum [7].…”

Section: Introductionmentioning

confidence: 98%

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Isolation of prekallikrein activator from guinea pig serum or plasma adsorbed to immune precipitates or celite: Possible relationship to Hageman factor

et al. 1972

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Immune aggregates of bovine serum albumin (BSA) and rabbit anti-BSA presumably adsorb Hageman factor (factor XII) and induce its conversion t o prekallikrein activator (PKA), which can be eluted from the precipitates and purified by chromatography. N o clotting studies could be done with the material desorbed from the immune aggregates incubated with serum, because thrombin was present in t h e preparations.When Al(OH)3-adsorbed plasma (free of prothrombin) was incubated with celite, large quantities of PKA were recovered in the celite eluates, together with activated factor XI1 (XIIa), activated factor XI (XIa) and kallikrein. These components could be separated by anion exchange chromatography and gel filtration. PKA had a molecular weight of approximately 31 000, 33 000 and 3 6 000 as determined by sucrose density gradient ultracentrifugation amino acid analysis and gel filtration, respectively; its sedimentation coefficient was 2.7 -2.9; in fully activated form it migrated as a sharp prealbumin band by disc gel electrophoresis. The isoelectric point of PKA was approximately 4.4.The moderately anionic factor XIIa had an estimated molecular weight of 120 000. The cationic factor XIa and kallikrein were separated by gel filtration, the clot-promoting substance having a molecular weight of 170 000 --180 000, while kallikrein was found t o be about 9 6 000. A kinin-forming, BAEe-hydrolysing fraction with an elution volume greater than that of egg albumin was recovered and it is assumed that it represents a fragment of kallikrein.It is concluded that during massive surface adsorption, most of the adsorbed factor XIIa becomes fragmented. This fragment acquires prekallikrein-activating activity. The fragment retains some of the property of the parent molecule by being able to partially correct the clotting defect of factor XIIdeficient plasma. These findings are in good agreement with those obtained under similar conditions with human plasma.

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Section: Discussionmentioning

confidence: 87%

“…[35] or the a,-macroglobulin which complexes with kallikrein [ 3 6 ] and probably with PKA [7]. Natural inhibitors of kinin have also been demonstrated [37].…”

Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 98%

See 1 more Smart Citation

Isolation of prekallikrein activator from guinea pig serum or plasma adsorbed to immune precipitates or celite: Possible relationship to Hageman factor

et al. 1972

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show abstract

“…(9) and Jahreis and Habermann (10) presented some evidence that factor XIIa acts 957 directly on prekallikrein. A prekallikrein activator distinct from factor XIIa and Pf/dil has been demonstrated first in guinea pig (11)(12)(13) and then in rabbit (14) and in human plasma (1,(15)(16)(17). I t was Kaplan and Austen ( 15) , who first proposed and presented some evidence that prekallikrein activator (PKA), a low molecular weight highly anionic substance, may represent a fragment of factor XIIa.…”

mentioning

confidence: 99%