The protein component of human brain thromboplastin

Bjørklid, Eirik; Storm, Eva; Prydz, Hans

doi:10.1016/0006-291x(73)91237-0

Cited by 73 publications

(35 citation statements)

References 14 publications

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“…Most of these findings are in general agreement with observations on the purification of the protein moieties of thromboplastin from other tissues [2,9,10,15,20,21]. The protein moiety of porcine lung thromboplastin differs from that of human brain thromboplastin with respect to the effect of dodecyl sulphate, thus preventing the use of this detergent in the purifica tion procedure.…”

Section: Discussionsupporting

confidence: 79%

“…This possibly explains the difference in the mole cular weight of the protein moiety of human brain thromboplastin observed by Bjorklid et al [2] (molecular weight 53,000) and by G onmori and Takeda [10] (molecular weight 200,000). The same might apply to the molecular weight of the protein moiety of bovine lung thromboplastin found by N emerson and Pitlick [21 ] (molecular weight 220,000 and 330,000) an by Liu and M cCoy [15] (molecular weight 56,000).…”

Section: Discussionmentioning

confidence: 79%

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Partial Purification of the Protein Moiety of Porcine Tissue Thromboplastin

Wijngaards¹,

Hemker²,

Deenen³

1977

Pathophysiol Haemos Thromb

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The tissue thromboplastin activity of porcine lung was separated from an aqueous tissue extract by differential centrifugation. Repeated suspension and sedimentation yielded a thromboplastin preparation free of soluble protein. The most effective delipidation of the lyophilized preparation with minimum denaturation of the protein moiety of thromboplastin was achieved using n-heptane/n-butanol extraction. A detergent was required to solubilize the thromboplastin protein moiety from the delipidated preparation. Gel filtration in the presence of detergent permitted further delipidation of the protein moiety and yielded a purified protein moiety. Apparent homogeneity was observed for the purified protein with several fractionation techniques. This apparently homogeneous protein dissociates into the constituent proteins in the presence of dodecyl sulphate. The aggregation of proteins is ascribed to their hydrophobic nature. Gel filtration on Bio-Gel A-1.5 m was found to be useful in the separation of the dodecyl sulphate-protein complexes on a preparative scale. Following the removal of the dodecyl sulphate, the renaturation of the thromboplastin protein moiety was unsuccessful. The purified protein moiety with its low lipid content (1 %) is suitable for lipid requirement studies.

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Section: Discussionsupporting

confidence: 79%

Section: Discussionmentioning

confidence: 79%

Partial Purification of the Protein Moiety of Porcine Tissue Thromboplastin

Wijngaards¹,

Hemker²,

Deenen³

1977

Pathophysiol Haemos Thromb

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“…Based on these results, we conclude that we have purified human tissue factor to an essentially homogeneous form, which has an apparent Mr of -46,000 as judged by NaDodSO4/PAGE with and without mercaptoethanol (not shown). This material is significantly different from previously described preparations of human brain tissue factor (19,20) in two important respects. First, it has a lower apparent Mr (46,000 vs. 53,000).…”

Section: Discussionmentioning

confidence: 45%

Affinity purification of human tissue factor: interaction of factor VII and tissue factor in detergent micelles.

Guha¹,

Bach²,

Konigsberg³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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Tissue factor, a known initiator of blood coagulation, was found to be active in Triton X-100. A system consisting of tissue factor, factor VIa, calcium ions, and coagulation factor X generated activated factor X at an appreciable rate. Based on this observation, we coupled human and bovine factor VII to a solid support. Each column bound tissue factor, solubilized in Triton X-100, in a species-specific manner. These interactions required calcium ions; when the columns were washed with detergent containing calcium ions,

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“…Each moiety is without procoagulant activity by itself, but mixing the apoprotein and phospholipid restores full thromboplastin ac tivity [1][2][3]. The species specificity of tissue thromboplastin has been known since early in the coagulation research period [4], Later, this phenomenon was studied by Stonnorken [5] and Irsigler et al [6], The latter showed that the species specificity resides in the pro tein moiety of thromboplastin [2].…”

Section: Introductionmentioning

confidence: 99%