Kinetic analysis of the fibrin monomers aggregation: Calculation of the fibrinogen-fibrin equilibrium constant

Usero, J.L.; Izquierdo, Carmen; Burguillo, F.J.; Roig, Manuel G.; Arco, Araceli del; Herraez, M. A.

doi:10.1016/0020-711x(81)90213-5

Cited by 6 publications

(4 citation statements)

References 23 publications

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“…[18][19][20] However, little research was focused on the kinetics of SF formation (i.e., fibrin monomer-fibrinogen interaction). [21][22][23][24] Our previous atomic force microscopy (AFM) studies 23 were mostly addressed to evaluate the strength of single FM-fibrin(ogen) pairs in terms of molecular interaction forces. It was demonstrated a strong specific interaction for fibrin-fibrin (ogen) complexes, which were formed by desAA-FM, desAABB-FM, synthetic knob A (GPRK 4 ), and fibrinogen.…”

Section: Introductionmentioning

confidence: 99%

“…Interestingly, to date, only one attempt was made to calculate the value of the equilibrium constant for the fibrinfibrinogen complex, K D . 22 In this earlier study K D was estimated spectrophotometrically (at an emission wavelength of 350 nm) from the time-dependent aggregation curves of fibrin monomers (0.647 M) in the presence of different fibrinogen concentrations (between 0 and 1.147 M). Nonetheless, the obtained value of K D (1.1 Â 10…”

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confidence: 99%

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Kinetics of the interaction of desAABB–fibrin monomer with immobilized fibrinogen

et al. 2006

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The soluble and stable fibrin monomer-fibrinogen complex (SF) is well known to be present in the circulating blood of healthy individuals and of patients with thrombotic diseases. However, its physiological role is not yet fully understood. To deepen our knowledge about this complex, a method for the quantitative analysis of interaction between soluble fibrin monomers and surface-immobilized fibrinogen has been established by means of resonant mirror (IAsys) and surface plasmon resonance (BIAcore) biosensors. The protocols have been optimized and validated by choosing appropriate immobilization procedures with regeneration steps and suitable fibrin concentrations. The highly specific binding of fibrin monomers to immobilized fibrin(ogen), or vice versa, was characterized by an affinity constant of approximately 10(-8)M, which accords better with the direct dissociation of fibrin triads (KD approximately 10(-8) -10(-9) M) (J. R. Shainoff and B. N. Dardik, Annals of the New York Academy of Science, 1983, Vol. 27, pp. 254-268) than with earlier estimations of the KD for the fibrin-fibrinogen complex (KD approximately 10(-6) M) (J. L. Usero, C. Izquierdo, F. J. Burguillo, M. G. Roig, A. del Arco, and M. A. Herraez, International Journal of Biochemistry, 1981, Vol. 13, pp. 1191-1196).

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Section: Introductionmentioning

confidence: 99%

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confidence: 99%

Kinetics of the interaction of desAABB–fibrin monomer with immobilized fibrinogen

et al. 2006

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“…However, little research was focused on the kinetics of SF formation (i.e., fibrin monomer–fibrinogen interaction) 21–24. Our previous atomic force microscopy (AFM) studies23 were mostly addressed to evaluate the strength of single FM–fibrin(ogen) pairs in terms of molecular interaction forces.…”

Section: Introductionmentioning

confidence: 99%

“…Nevertheless, these single molecule techniques (AFM and optical tweezers) alone cannot yield information about such parameters as the equilibrium constant and/or association rate constant. Interestingly, to date, only one attempt was made to calculate the value of the equilibrium constant for the fibrin–fibrinogen complex, K D 22. In this earlier study K D was estimated spectrophotometrically (at an emission wavelength of 350 nm) from the time‐dependent aggregation curves of fibrin monomers (0.647 μ M ) in the presence of different fibrinogen concentrations (between 0 and 1.147 μ M ).…”

Section: Introductionmentioning

confidence: 99%

Spinocerebellar ataxia type 17: Extension of phenotype with putaminal rim hyperintensity on magnetic resonance imaging

Loy¹,

Sweeney²,

Davis³

et al. 2005

Movement Disorders

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We report on a 50-year-old woman who presented with an 8-year history of involuntary movements, unsteadiness, and cognitive decline. Examination revealed multidomain cognitive deficits, jerky ocular pursuit movements, hypometric saccades, gaze impersistence, dysarthria, upper limb dystonia, and widespread chorea. TATA-binding protein gene test revealed trinucleotide expansion allele sizes of 47 and 39 repeats, confirming the diagnosis of spinocerebellar ataxia type 17 (SCA-17). Magnetic resonance imaging (MRI) showed marked cerebellar atrophy and putaminal rim hyperintensity. This is the first case of SCA-17 reported to show MRI signal change in the basal ganglia, and extends the phenotypic manifestation of SCA-17.

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A mechanism for fibrin monomer aggregation based on a kinetic study

Usero¹,

Burguillo²,

Izquierdo³

et al. 1984

International Journal of Biochemistry

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Kinetic analysis of the fibrin monomers aggregation: Calculation of the fibrinogen-fibrin equilibrium constant

Cited by 6 publications

References 23 publications

Kinetics of the interaction of desAABB–fibrin monomer with immobilized fibrinogen

Kinetics of the interaction of desAABB–fibrin monomer with immobilized fibrinogen

Spinocerebellar ataxia type 17: Extension of phenotype with putaminal rim hyperintensity on magnetic resonance imaging

A mechanism for fibrin monomer aggregation based on a kinetic study

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