Adsorption of fibrinogen derivatives on insolubilized fibrinogen and fibrinmonomer

Heene, D. L.; Matthias, Fritz Reinhard

doi:10.1016/0049-3848(73)90025-x

Cited by 148 publications

(49 citation statements)

References 10 publications

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“…6, in which fibrin is represented as a two-stranded, half-staggered overlap fiber, with noncovalent attractions between D and E domains of adjacent fibrin strands (48,49). Whereas complex 1 would derive from fragment DD of one fibrin strand and fragment E from the adjacent strand, joined by noncovalent attraction, complex 2 would consist of two antiparallel DY fragments, held together by the same noncovalent bond between adjacent DD and E regions.…”

Section: Discussionmentioning

confidence: 99%

Plasmic Degradation of Crosslinked Fibrin

Francis¹,

Marder²,

Barlow³

1980

J. Clin. Invest.

123

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A B S T R A C T Crosslinked fibrin was digested by plasmin, and three soluble complexes larger than DD/E were purified and characterized. After gel filtration chromatography, the purified complexes were shown to have molecular weights of 465,000, 703,000, and 850,000, as determined by equilibrium sedimentation. Each of the complexes was dissociated into two or more fragments by SDS-polyacrylamide gel electrophoresis. The structure of these subunit fragments was deduced from determinations of their molecular weights and polypeptide chain composition and from known sites of plasmin cleavage of fibrin. Fragments larger than DD have been identified that contain intact yry crosslinks as well as fragments resulting from cleavages at or near this site. The former include DY (mol wt 247,000), YY (mol wt 285,000), DXD (mol wt 461,000), and YXD (mol wt 500,000); and the latter include fragments XD (mol wt 334,000) and XY (mol wt 391,000). A schematic model was developed to explain the structure of the large noncovalently bound complexes based on their molecular weight and observed component fragments. Our scheme supports the twostranded half-staggered overlap model as the basic unit of fibrin structure, in which each complex consists of fragments from two adjacent complementary antiparallel fibrin strands. The smallest derivative, complex 1, is the DD/E complex; complex 2 contains apposed DY and YD fragments, and complex 3 consists of fragments DXD and YY. Complex 4 is less wellcharacterized, but its intact structure is projected to consist of YXD and DXY fragments from adjacent fibrin strands. Each complex is heterogeneous in subunit composition, reflecting additional plasmin cleavages within and/or adjacent to its theoretical boundaries. Since most ofthe protein initially released into solution from degrading fibrin is as complexes larger than DD/E,

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Section: Discussionmentioning

confidence: 99%

Plasmic Degradation of Crosslinked Fibrin

Francis¹,

Marder²,

Barlow³

1980

J. Clin. Invest.

123

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“…Total release of fibrino-peptides by either thrombin or Reptilase and aggregation of fibrin monomer were studied essentially according to Gralnick et al (19) Binding study using Sepharose conjugated with fibrin monomer or with plasmic digests of cross-linked fibrin. Fibrinmonomer-Sepharose was prepared from normal fibrinogen essentially according to Heene and Matthias (25), packed into a small column (gel vol = 4 ml), and equilibrated with 0.05 M Tris-H3PO4, pH 7.6, containing 0.1 M NaCI, 0.005 M EDTA, and 5 KIU/ml aprotinin (buffer A). A gradient employing pH (7.6 -4.1) and NaCl (0.1 a 2.0 M) was applied for elution using 0.05 M Tris-H3PO4, pH 4.1, containing 2.0 M NaCl, 0.005 M EDTA, and 5 KIU/ml aprotinin (buffer B1).…”

Section: Methodsmentioning

confidence: 99%

"Fibrinogen Tokyo II". An abnormal fibrinogen with an impaired polymerization site on the aligned DD domain of fibrin molecules.

Matsuda¹,

Baba²,

Morimoto³

et al. 1983

J. Clin. Invest.

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A B S T R A C T A hereditary dysfibrinogenemia associated with defective aggregation of fibrin monomers was found in a 39-yr-old female and in the members of her immediate family, who had all been asymptomatic.The abnormality was probably due to an impaired polymerization site exposed in the DD domain of two adjacent fibrin molecules, because plasmic fragment DD derived from the propositus' cross-linked fibrin bound far less tightly to insolubilized normal fragment E than that from the normal one. Its complementary polymerization site in the E domain of fibrin, which was exposed by thrombin cleavage, and the polymerization site in the D domain of fibrinogen, which was available without activation by thrombin, were both found to be normal.More anodal migration of the abnormal fragment DD than the normal one, as shown by immunoelectrophoresis, seemed to support our concept that the mutation most likely resides in the D domain of the abnormal fibrinogen molecule at or near a region closely related to the polymerization site that is exposed when two fibrin molecules are linearly aligned.The work of others on the polymerization of normal fibrin with different techniques yielded results consistent with our conclusions.We tentatively designate this type of abnormal fibrinogen "fibrinogen Tokyo II," but its possible identity with other abnormalities of fibrinogen reported heretofore is not excluded.

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“…), the fibrinogen emerged in a single symmetrical peak; the "ethanol gelation" test (25) was negative; no cryoprecipitate formned upon incubation at 2-4°C. Occasional preparations giving evidence of small amounts of "fibrin" or aggregates by one or more of the above criteria were subjected to chromatography at room temperature on a 0.9 x 25-cm fibrinogen-Sepharose affinity column (26); in such a system fibrin selectively binds to the column. After this additional treatment, the material met all the criteria described above for fibrinfree fibrinogen, and behaved in the same way as fibrinogen preparations not requiring such treatment.…”

Section: Methodsmentioning

confidence: 99%