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Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen)

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Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen). / Greenberg, C S; Enghild, J J; Mary, A; Dobson, J V; Achyuthan, K E.

In: Biochemical Journal, Vol. 256, No. 3, 1988, p. 1013-9.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Greenberg, CS, Enghild, JJ, Mary, A, Dobson, JV & Achyuthan, KE 1988, 'Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen)', Biochemical Journal, vol. 256, no. 3, pp. 1013-9.

APA

Greenberg, C. S., Enghild, J. J., Mary, A., Dobson, J. V., & Achyuthan, K. E. (1988). Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen). Biochemical Journal, 256(3), 1013-9.

CBE

Greenberg CS, Enghild JJ, Mary A, Dobson JV, Achyuthan KE. 1988. Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen). Biochemical Journal. 256(3):1013-9.

MLA

Vancouver

Greenberg CS, Enghild JJ, Mary A, Dobson JV, Achyuthan KE. Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen). Biochemical Journal. 1988;256(3):1013-9.

Author

Greenberg, C S ; Enghild, J J ; Mary, A ; Dobson, J V ; Achyuthan, K E. / Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen). In: Biochemical Journal. 1988 ; Vol. 256, No. 3. pp. 1013-9.

Bibtex

@article{b476f660864a11dda5a8000ea68e967b,
title = "Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen)",
abstract = "Purified platelet Factor XIII was radioiodinated and then partially degraded by thrombin or trypsin, and a fibrin-binding fragment was identified by autoradiography and immunoblotting following separation by SDS/polyacrylamide-gel electrophoresis. Limited proteolysis of 125I-Factor XIII by thrombin or trypsin produced an 125I-51 kDa fragment and an unlabelled 19 kDa fragment. The 51 kDa fragment was purified by h.p.l.c. on a TSK-125 gel-filtration column. Partial amino acid sequence analysis of the 51 kDa fragment indicated that it was similar in sequence to the Gly38-Lys513 segment in placental Factor XIII a-chain. More than 70{\%} of the 51 kDa fragment bound to fibrin, whereas the 19 kDa fragment did not bind. The active site was localized to the 51 kDa fragment since this fragment expressed transglutaminase activity, cross-linked fibrin and fibrinogen and incorporated iodo[14C]acetamide into the active-site cysteine residue. Isolation of a fibrin-binding fragment expressing transglutaminase activity demonstrates that each a-chain of the dimeric Factor XIIIa could function independently to cross-link fibrin. The fibrin-binding site could play an important role in localizing Factor XIIIa to the fibrin clot.",
keywords = "Amino Acid Sequence, Binding Sites, Cross-Linking Reagents, Factor XIII, Fibrin, Fibrinogen, Humans, Molecular Sequence Data, Peptide Fragments, Peptide Hydrolases",
author = "Greenberg, {C S} and Enghild, {J J} and A Mary and Dobson, {J V} and Achyuthan, {K E}",
year = "1988",
language = "English",
volume = "256",
pages = "1013--9",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "3",

}

RIS

TY - JOUR

T1 - Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen)

AU - Greenberg, C S

AU - Enghild, J J

AU - Mary, A

AU - Dobson, J V

AU - Achyuthan, K E

PY - 1988

Y1 - 1988

N2 - Purified platelet Factor XIII was radioiodinated and then partially degraded by thrombin or trypsin, and a fibrin-binding fragment was identified by autoradiography and immunoblotting following separation by SDS/polyacrylamide-gel electrophoresis. Limited proteolysis of 125I-Factor XIII by thrombin or trypsin produced an 125I-51 kDa fragment and an unlabelled 19 kDa fragment. The 51 kDa fragment was purified by h.p.l.c. on a TSK-125 gel-filtration column. Partial amino acid sequence analysis of the 51 kDa fragment indicated that it was similar in sequence to the Gly38-Lys513 segment in placental Factor XIII a-chain. More than 70% of the 51 kDa fragment bound to fibrin, whereas the 19 kDa fragment did not bind. The active site was localized to the 51 kDa fragment since this fragment expressed transglutaminase activity, cross-linked fibrin and fibrinogen and incorporated iodo[14C]acetamide into the active-site cysteine residue. Isolation of a fibrin-binding fragment expressing transglutaminase activity demonstrates that each a-chain of the dimeric Factor XIIIa could function independently to cross-link fibrin. The fibrin-binding site could play an important role in localizing Factor XIIIa to the fibrin clot.

AB - Purified platelet Factor XIII was radioiodinated and then partially degraded by thrombin or trypsin, and a fibrin-binding fragment was identified by autoradiography and immunoblotting following separation by SDS/polyacrylamide-gel electrophoresis. Limited proteolysis of 125I-Factor XIII by thrombin or trypsin produced an 125I-51 kDa fragment and an unlabelled 19 kDa fragment. The 51 kDa fragment was purified by h.p.l.c. on a TSK-125 gel-filtration column. Partial amino acid sequence analysis of the 51 kDa fragment indicated that it was similar in sequence to the Gly38-Lys513 segment in placental Factor XIII a-chain. More than 70% of the 51 kDa fragment bound to fibrin, whereas the 19 kDa fragment did not bind. The active site was localized to the 51 kDa fragment since this fragment expressed transglutaminase activity, cross-linked fibrin and fibrinogen and incorporated iodo[14C]acetamide into the active-site cysteine residue. Isolation of a fibrin-binding fragment expressing transglutaminase activity demonstrates that each a-chain of the dimeric Factor XIIIa could function independently to cross-link fibrin. The fibrin-binding site could play an important role in localizing Factor XIIIa to the fibrin clot.

KW - Amino Acid Sequence

KW - Binding Sites

KW - Cross-Linking Reagents

KW - Factor XIII

KW - Fibrin

KW - Fibrinogen

KW - Humans

KW - Molecular Sequence Data

KW - Peptide Fragments

KW - Peptide Hydrolases

M3 - Journal article

VL - 256

SP - 1013

EP - 1019

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 3

ER -