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Title: Proton NMR study of the state of water in fibrin gels, plasma, and blood clots

Abstract

A proton NMR relaxation and pulsed field gradient self-diffusion study of water in fibrin gels, plasma, and blood clots has been performed with special emphasis on the effect of the sol-gel and shrinkage transitions. Deuteron NMR in fibrin gels was also studied to supplement the proton data. It is shown that a measurement of the water proton or deuteron T1/T2 ratio allows for a determination of the bound water fraction in all these systems. The change in the T1/T2 ratio at the shrinkage transition further allows for a determination of the surface fractal dimension of the gel if the change in the volume of the gel is known. The self-diffusion coefficient of water in these systems, which determines the transport properties of the gel, is found to be proportional to the free water fraction in both the nonshrunken and shrunken state.

Authors:
; ; ; ;  [1]
  1. (Univ. Institute of Gerontology, Ljubjana (Yugoslavia))
Publication Date:
OSTI Identifier:
6709079
Alternate Identifier(s):
OSTI ID: 6709079
Resource Type:
Journal Article
Resource Relation:
Journal Name: Magnetic Resonance in Medicine; (USA); Journal Volume: 14:1
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; BODY FLUIDS; NMR SPECTRA; BLOOD COAGULATION; BLOOD PLASMA; DEUTERIUM; FIBRIN; FIBRINOGEN; FREEZING; MAN; NUCLEAR MAGNETIC RESONANCE; PROTONS; TRACER TECHNIQUES; ANIMALS; BARYONS; BIOLOGICAL MATERIALS; BLOOD; BLOOD COAGULATION FACTORS; COAGULANTS; DRUGS; ELEMENTARY PARTICLES; FERMIONS; GLOBULINS; HADRONS; HEMATOLOGIC AGENTS; HEMOSTATICS; HYDROGEN ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; LIGHT NUCLEI; MAGNETIC RESONANCE; MAMMALS; MATERIALS; NUCLEI; NUCLEONS; ODD-ODD NUCLEI; ORGANIC COMPOUNDS; PRIMATES; PROTEINS; RESONANCE; SCLEROPROTEINS; SPECTRA; STABLE ISOTOPES; VERTEBRATES 550201* -- Biochemistry-- Tracer Techniques

Citation Formats

Blinc, A., Lahajnar, G., Blinc, R., Zidansek, A., and Sepe, A. Proton NMR study of the state of water in fibrin gels, plasma, and blood clots. United States: N. p., 1990. Web. doi:10.1002/mrm.1910140111.
Blinc, A., Lahajnar, G., Blinc, R., Zidansek, A., & Sepe, A. Proton NMR study of the state of water in fibrin gels, plasma, and blood clots. United States. doi:10.1002/mrm.1910140111.
Blinc, A., Lahajnar, G., Blinc, R., Zidansek, A., and Sepe, A. Sun . "Proton NMR study of the state of water in fibrin gels, plasma, and blood clots". United States. doi:10.1002/mrm.1910140111.
@article{osti_6709079,
title = {Proton NMR study of the state of water in fibrin gels, plasma, and blood clots},
author = {Blinc, A. and Lahajnar, G. and Blinc, R. and Zidansek, A. and Sepe, A.},
abstractNote = {A proton NMR relaxation and pulsed field gradient self-diffusion study of water in fibrin gels, plasma, and blood clots has been performed with special emphasis on the effect of the sol-gel and shrinkage transitions. Deuteron NMR in fibrin gels was also studied to supplement the proton data. It is shown that a measurement of the water proton or deuteron T1/T2 ratio allows for a determination of the bound water fraction in all these systems. The change in the T1/T2 ratio at the shrinkage transition further allows for a determination of the surface fractal dimension of the gel if the change in the volume of the gel is known. The self-diffusion coefficient of water in these systems, which determines the transport properties of the gel, is found to be proportional to the free water fraction in both the nonshrunken and shrunken state.},
doi = {10.1002/mrm.1910140111},
journal = {Magnetic Resonance in Medicine; (USA)},
number = ,
volume = 14:1,
place = {United States},
year = {Sun Apr 01 00:00:00 EST 1990},
month = {Sun Apr 01 00:00:00 EST 1990}
}
  • Factors effecting the polymerization of fibrin are briefly reviewed, and it is shown that a preliminary x irradiation modifies the polymerization and therefore the clot structure. ln order to determine whether the dependency between clot structure and pH is also present in irradiated plasma, blood plasma was irradiated at different pH values. The results show that at a given pH the clot transparency in the irradiated samples is much larger than in unirradiated samples. The reasons for the variation in the optical density of the clots were studied and possible solutions were suggested.
  • In order to estimate the solubility of contaminating fibrin in CPD-blood, thrombin induced fibrin polymerzation in CPD-plasma was examined by light scattering and fibrinopeptide A (FPA) determinations. In addition, I-125 fibrin monomer enriched CPD-blood was used to investigate fibrin monomer retention in blood bags and transfusion filters (170 microns) and fibrin distribution in blood components derived from CPD-blood. Initial fibrin polymerization in CPD-blood occurred after conversion of 15 per cent of the fibrinogen to fibrin, implying that substantial amounts of fibrin may be kept solubilized in CPD-blood bags. Only minor amounts of I-125 fibrin monomers were retained in blood bagsmore » (2.4 per cent) and in transfusion filters (2.9 per cent) after sham transfusions. After separating I-125-fibrin monomer enriched CPD-blood into its constituent components, the major part of fibrin (75.0 per cent) could be traced in the cryoprecipitate.« less
  • The purpose of this article is to review some of the NMR techniques used to measure /sup 1/H NMR spectra of human plasma and red blood cells. The /sup 1/H NMR spectroscopy of plasma and red blood cells of interest because reported studies indicate that information relevant to biochemical and clinical applications can be obtained by /sup 1/H NMR.
  • Clots formed in reconstituted human plasma or from purified human fibrin were studied in order to assess the effects of subunit crosslinking on clot strength and on resistance to plasmin degradation. The relative amounts of alpha chain and gamma chain ligation were varied by adding factor XIII to the samples. We observe, as have others, that appreciable gamma-gamma crosslinking always precedes detectable formation of alpha dimer or alpha polymer. Non-invasive light scattering measurements of the shear modulus G(t) indicate that ligation of gamma chains and of alpha chains have qualitatively similar effects on clot strength. Since alpha crosslinking occurs verymore » slowly in the clots which are formed from plasma, we infer that under physiological conditions the involvement of alpha chains in the development of clot strength probably is only a secondary function. Light scattering techniques also were used to study the size of particles shed from the surfaces of fibrin clots undergoing fibrinolysis, and no differences could be discerned as resulting from ligation of alpha chains.« less
  • Interaction of tissue plasminogen activator (t-PA) with fibrin plays a key role in regulation of plasminogen activation and clot dissolution. Previous investigations of t-PA-fibrin interaction, using incorporation of t-PA into polymerizing fibrin clots, have suggested that no significant differences exist in the binding of one-chain or two-chain t-PA to non-cross-linked or cross-linked fibrin. In the present study, binding of 125I-labeled and affinity-purified one-chain and two-chain forms of t-PA to preformed non-cross-linked or cross-linked, sonicated suspension of fibrin was investigated. Interaction of one-chain t-PA with cross-linked fibrin involved a single type of binding site with dissociation constant (kd) of 0.58 mumol/Lmore » and a stoichiometry (n) of 1.5. Interaction of one-chain t-PA with non-cross-linked fibrin, however, involved two classes of binding sites with dissociation constants of 0.32 and 1.5 mumol/L and corresponding number of binding sites equal to 0.57 and 2.0, respectively. In contrast to the binding of one-chain t-PA to cross-linked fibrin by a limited number of sites, two-chain t-PA appeared to involve a considerably greater number of sites (minimum six) whose dissociation constant was 3.2 mumol/L. Interaction of two-chain t-PA with non-cross-linked fibrin also showed the presence of many binding sites (minimum seven) with approximate dissociation constant of 6.4 mumol/L, as well as a few (n = 0.012) high-affinity sites with a kd of 0.011 mumol/L epsilon-Aminocaproic acid did not completely reverse the binding of either one-chain t-PA or two-chain t-PA to fibrin. The present findings suggest that the fibrin-binding properties of t-PA undergo considerable changes on proteolytic conversion from one-chain to two-chain t-PA, catalyzed under physiologic conditions by plasmin.« less