Isolation and properties of an abnormal Hageman factor (Factor XII) molecule in a cross-reacting material-positive hageman trait plasma.

Saito, Hidehiko; Scialla, Salvatore J.

doi:10.1172/jci110325

Cited by 18 publications

(13 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…11 We have isolated nonfunctional abnormal Factor XII (HF) from plasma of one of these CRM + subjects and compared it with the normal molecule (Table 3). 115 Abnormal HF had similar molecular weights (MW), isoelectric point (pI), and amino acid composition to normal HF, and it was as readily absorbed to negatively charged surfaces as normal HF and underwent an identical pattern of cleavage after contact activation in normal plasma or tryptic digestion. On the digestion by trypsin, however, the abnormal HF did not incorporate diisopropylfluorophosphate ([ 3 H] DFP) into its 29,000 MW fragment (a light chain), whereas normal HF did.…”

Section: Hereditary Disorders Of the Contact Factors Factor XII (Hagementioning

confidence: 99%

Contact Factors in Health and Disease

Saito¹

1987

Semin Thromb Hemost

View full text Add to dashboard Cite

Section: Hereditary Disorders Of the Contact Factors Factor XII (Hagementioning

confidence: 99%

Contact Factors in Health and Disease

Saito¹

1987

Semin Thromb Hemost

View full text Add to dashboard Cite

“…In 1 case [6], nonprekallikrein-activating activ ity was generated after cleavage of the Hageman factor molecule with trypsin. Another showed a lack of preotease activity on the kallikreincleaved molecule [5], In still another case [4], the abnormal FXII molecule was very slowly ac tivated after binding to negatively charged surfaces.…”

mentioning

confidence: 99%

Functional Anomaly of Factor XII

Aznar¹,

Villa²,

Vayá³

et al. 1992

Pathophysiol Haemos Thromb

View full text Add to dashboard Cite

“…The isoelectric focusing pattern of normal and dysfunctional F XI1 was identical, showing several distinct isoelectric forms with PIS between 5.9 and 6.8 (Fig l), in agreement with other reports on purified normal F XII. 18,37 These data indicate that F XI1…”

Section: Discussionmentioning

confidence: 87%

Functional characterization of an abnormal factor XII molecule (F XII Bern)

Wuillemin

Huber

Furlan

et al. 1991

Blood

View full text Add to dashboard Cite

An 18-year-old healthy woman was found to have cross-reacting material (CRM)-positive factor XII (F XII) deficiency, F XII clotting activity was less than 0.01 U/mL, whereas F XII antigen was 0.11 U/mL. An F XII inhibitor was excluded. To partially characterize the molecular defect of the abnormal F XII, immunologic and functional studies were performed on the proposita's plasma. The abnormal F XII was a single chain molecule with the same molecular weight (80 Kd) and the same isoelectric points (pl, 5.9 to 6.8) as normal F XII. Dextran sulfate activation of the proposita's plasma showed no proteolytic cleavage of F XII even after 120 minutes, whereas F XII in pooled normal plasma, diluted 1:10 with CRM-negative F XII-deficient plasma, was completely cleaved after 40 minutes. Adsorption to kaolin was identical for both abnormal and normal F XII. In the presence of dextran sulfate and exogenous plasma kallikrein, the abnormal F XII was cleaved with the same rate as normal F XII. However, kallikrein-cleaved abnormal F XII was not able to cleave factor XI and plasma prekallikrein, in contrast to activated normal F XII. Thus, these studies show that the functional defect of this abnormal F XII, denoted as F XII Bern, is due to the lack of protease activity of the kallikrein-cleaved molecule. Therefore, the structural defect is likely to be located in the light chain region of F XII, containing the enzymatic active site.

show abstract

Isolation and properties of an abnormal Hageman factor (Factor XII) molecule in a cross-reacting material-positive hageman trait plasma.

Cited by 18 publications

References 26 publications

Contact Factors in Health and Disease

Contact Factors in Health and Disease

Functional Anomaly of Factor XII

Functional characterization of an abnormal factor XII molecule (F XII Bern)

Contact Info

Product

Resources

About