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Electron microscopy and hydrodynamic properties of factor XIII subunits.

Publication ,  Journal Article
Carrell, NA; Erickson, HP; McDonagh, J
Published in: J Biol Chem
January 5, 1989

Factor XIII is a transglutaminase important in blood coagulation and fibrinolysis. Its function is to catalyze peptide bond formation between the gamma-carboxamide group of glutamines in one protein and the epsilon-amino group of lysine in another. There are two zymogenic forms of factor XIII: one is a noncovalent, intracellular dimer (A2); the other is a noncovalent, extracellular tetramer (A2B2). The catalytic function resides in the activated A chain (A2.). Purified forms of factor XIII (A2B2, A2, A2.B2, B) were prepared and analyzed by electron microscopy, gel filtration, and gradient centrifugation. Hydrodynamic constants were derived. Electron microscopy of rotary-shadowed molecules showed A2 to consist of two globular particles each about 6 x 9 nm in size. The A2 dimer is significantly elongated, 18 nm long and 6 nm in diameter. Sedimentation and gel filtration of the A2 dimer are consistent with this asymmetric structure. B protein is a filamentous, flexible strand with kinks, with a contour length of 30 nm and a diameter of approximately 2-3 nm. The sedimentation and gel filtration behavior of the B subunit are characteristic of a highly asymmetric molecule. The observed structure of the B subunit, combined with data for its amino acid sequence, suggests a modular structure. The B subunit is a member of a family of proteins composed of tandem, repeating structures (referred to as GP-I domains); the structure seen by electron microscopy for B subunit is probably applicable to all proteins in this family. Plasma and platelet factor XIII zymogens are tetrameric and dimeric, but B protein, in the absence of A protein, appears to be monomeric. Our model for the A2B2 zymogen has the elongated A2 dimer forming the core and the two B strands wrapping around the outside.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

January 5, 1989

Volume

264

Issue

1

Start / End Page

551 / 556

Location

United States

Related Subject Headings

  • Models, Molecular
  • Microscopy, Electron
  • Humans
  • Glutaral
  • Factor XIII
  • Electrophoresis, Polyacrylamide Gel
  • Chromatography, Gel
  • Centrifugation, Density Gradient
  • Biochemistry & Molecular Biology
  • 34 Chemical sciences
 

Citation

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Carrell, N. A., Erickson, H. P., & McDonagh, J. (1989). Electron microscopy and hydrodynamic properties of factor XIII subunits. J Biol Chem, 264(1), 551–556.
Carrell, N. A., H. P. Erickson, and J. McDonagh. “Electron microscopy and hydrodynamic properties of factor XIII subunits.J Biol Chem 264, no. 1 (January 5, 1989): 551–56.
Carrell NA, Erickson HP, McDonagh J. Electron microscopy and hydrodynamic properties of factor XIII subunits. J Biol Chem. 1989 Jan 5;264(1):551–6.
Carrell, N. A., et al. “Electron microscopy and hydrodynamic properties of factor XIII subunits.J Biol Chem, vol. 264, no. 1, Jan. 1989, pp. 551–56.
Carrell NA, Erickson HP, McDonagh J. Electron microscopy and hydrodynamic properties of factor XIII subunits. J Biol Chem. 1989 Jan 5;264(1):551–556.

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

January 5, 1989

Volume

264

Issue

1

Start / End Page

551 / 556

Location

United States

Related Subject Headings

  • Models, Molecular
  • Microscopy, Electron
  • Humans
  • Glutaral
  • Factor XIII
  • Electrophoresis, Polyacrylamide Gel
  • Chromatography, Gel
  • Centrifugation, Density Gradient
  • Biochemistry & Molecular Biology
  • 34 Chemical sciences