Permeability Enhancing and Chemotactic Activities of Lower Molecular Weight Degradation Products of Human Fibrinogen

1981 ◽  
Vol 45 (01) ◽  
pp. 090-094 ◽  
Author(s):  
Katsuo Sueishi ◽  
Shigeru Nanno ◽  
Kenzo Tanaka
Keyword(s):  
Molecular Weight ◽  
Degradation Products ◽  
Electron Microscopic Observation ◽  
Chemotactic Activity ◽  
Lower Molecular Weight ◽  
Electron Microscopic ◽  
Human Fibrinogen ◽  
Rabbit Skin ◽  
Molecular Weights ◽  
Active Fragments

SummaryFibrinogen degradation products were investigated for leukocyte chemotactic activity and for enhancement of vascular permeability. Both activities increased progressively with plasmin digestion of fibrinogen. Active fragments were partially purified from 24 hr-plasmin digests. Molecular weights of the permeability increasing and chemotactic activity fractions were 25,000-15,000 and 25,000 respectively. Both fractions had much higher activities than the fragment X, Y, D or E. Electron microscopic observation of the small blood vessels in rabbit skin correlated increased permeability with the formation of characteristic gaps between adjoining endothelial cells and their contraction.These findings suggest that lower molecular weight degradation products of fibrinogen may be influential in contributing to granulocytic infiltration and enhanced permeability in lesions characterized by deposits of fibrin and/or fibrinogen.

Permeability Enhancing And Chemotactic Activities Of Lower Molecular Weight Degradation Products Of Human Fibrinogen

1981 ◽  
Author(s):  
K Tanaka ◽  
K Sueishi
Keyword(s):  
Molecular Weight ◽  
Vascular Permeability ◽  
Degradation Products ◽  
Chemotactic Activity ◽  
Lower Molecular Weight ◽  
Boyden Chamber ◽  
Electron Microscopic ◽  
Human Fibrinogen ◽  
Rabbit Skin ◽  
Vascular Walls

Fibrinogen degradation products were investigated for leukocyte chemotactic activity and enhancement of vascular permeability. Fragments X, Y, D and E, and non-dialysable lower molecular weight degradation products were fractionated from plasmin digests of human fibrinogen by gel filtration, zone electrophoresis and ion exchange chromatography. They were assayed for chemotactic activity for human granulocytes by the modified Boyden chamber and for vascular permeability increasing activity in rabbit skin injected intravenously with pontamine blue.Both activities increased progressively with plasmin digestion of fibrinogen. Molecular weights of the permeability increasing and chemotactic activity fractions were 25,000-15,000 and 25,000 respectively. Both fractions had much higher activities than the fragment X, Y, D and E. The low molecular weight break down product with chemotactic activity showed the highest activity in rabbit skin in vivo as well. Granulocytic infiltration was most prominent 6-12 hr after intradermal injection and apparent even at an intradermal dose of 0.5/μg. Permeability enhancement of the active fraction reached to its muximum level at 5-10 min and was dose-dependent. Electron microscopic observations of the small blood vessels in rabbit skin correlated an increased permeability with the formation of characteristic gaps between adjacent endothelial cells and their contraction. Carbon particles used as a tracer passed into the vascular walls through these intercellular gaps.These observations add more support for the hypothesis that lower molecular weight degradation products of fibrinogen may be influential in contributing to granulocytic infiltration and enhanced permeability in lesions associated with deposits of fibrin and/or fibrinogen.

Comparison of Electron and Infrared Spectroscopy with Thermal Analysis to Study Molecular Weight Effects in PVC-PMMA Blends

1993 ◽  
Vol 47 (10) ◽  
pp. 1636-1642 ◽  
Author(s):  
Cindy A. Burkhardt ◽  
Joseph A. Gardella
Keyword(s):  
Thermal Analysis ◽  
Molecular Weight ◽  
Differential Scanning Calorimetry ◽  
Infrared Spectroscopy ◽  
Lower Molecular Weight ◽  
Scanning Calorimetry ◽  
Molecular Weights ◽  
Solvent Cast ◽  
Pmma Blends

The effects of homopolymer molecular weight on the miscibility of PVC/PMMA solvent cast blends were studied. Two significantly different molecular weights were chosen for each of the homopolymers, and a series of blends was prepared from the four possible homopolymer-homopolymer combinations. Angle-dependent ESCA results suggest that the surfaces of the blends are enriched with PMMA. The extent of this enrichment is dependent on molecular weight, with the most enrichment seen in blends containing the lower-molecular-weight PMMA homopolymer. Differential scanning calorimetry (DSC) results are also presented.

scholarly journals Structural Characterization, Antioxidant Activity, and Biomedical Application of Astragalus Polysaccharide Degradation Products

2018 ◽  
Vol 2018 ◽  
pp. 1-13 ◽  
Author(s):  
Jian-Min Wang ◽  
Xin-Yuan Sun ◽  
Jian-Ming Ouyang
Keyword(s):  
Molecular Weight ◽  
Antioxidant Activity ◽  
Biomedical Application ◽  
Degradation Products ◽  
Human Kidney ◽  
Degradation Process ◽  
Chain Structure ◽  
Molecular Weights ◽  
Reducing Ability

To study the antioxidant capacity of Astragalus polysaccharides (APS) with different molecular weights, we used hydrogen peroxide to degrade original Astragalus polysaccharide (APS0) with an initial molecular weight of 11.03 kDa and obtained three degraded polysaccharides with molecular weights of 8.38 (APS1), 4.72 (APS2), and 2.60 kDa (APS3). The structures of these polysaccharides were characterized by 1H NMR, 13C NMR, FT-IR, and GC/MS. The degradation process did not cause significant changes in the main chain structure of APS. The monosaccharide component of APS before and after degradation was slightly changed. The antioxidant ability in vitro (removing hydroxyl and ABTS radicals and reducing ability) and in cells (superoxide dismutase and malondialdehyde generation) of these polysaccharides is closely related to their molecular weight. If the molecular weight of APS is very high or low, it is not conducive to their activity. Only APS2 with moderate molecular weight showed the greatest antioxidant activity and ability to repair human kidney epithelial (HK-2) cells. Therefore, APS2 can be used as a potential antistone polysaccharide drug.

A Simple and Practical Method for Isolation of an Early Plasmin Degradation Product of Human Fibrinogen

1977 ◽  
Vol 37 (03) ◽  
pp. 464-470 ◽  
Author(s):  
Kimiteru Takagi ◽  
Tadashi Kawai
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Degradation Product ◽  
Degradation Products ◽  
Practical Method ◽  
Human Fibrinogen ◽  
Simple Method ◽  
Hydrophobic Amino Acids ◽  
Very High

SummaryOne of the earliest plasmin degradation products of human fibrinogen, so-called fragment A, was isolated by a simple method.This peptide has a molecular weight of approximately 22,500, migrating electrophoretically at beta-area, and its amino acid composition shows a very high content of glycine, serine, threonine and proline, and a markedly low content of hydrophobic amino acids. This fragment does not react against anti-fibrinogen; however, the anti-serum of this fragment reacts strongly with fibrinogen.

scholarly journals Generation of Fibrinogen Degradation Products (FDP’s) by Neutral Proteases from Human Granulocytes and their Importance for the Blood Clotting System

1977 ◽  
Author(s):  
M. Gramse ◽  
Ch. Bingenheimer ◽  
R. Egbring ◽  
K. Havemann
Keyword(s):  
Molecular Weight ◽  
Blood Clotting ◽  
Degradation Products ◽  
Enzyme Concentration ◽  
Antigenic Determinants ◽  
Clotting System ◽  
Human Fibrinogen ◽  
Human Granulocytes ◽  
Antigen Antibody ◽  
Neutral Proteases

The effect of neutral proteases from human granulocytes (elastase-like and chymotrypsin-like protease) on purified human fibrinogen was investigated. Detectable by two-dimensional and Polyacrylamide electrophoresis, dependence of fibrinogen degradation of enzyme concentration and incubation time was found. Molecular weight of the FDP’s was estimated by gelchromatografy. Some greater FDP’s showed the antigenic determinants of fibrinogen and of the split products D and E. High molecular weight FDP’s inhibited fibrinogen clotting. Generated at high enzyme concentrations and longer incubation times, FDP’s lost their ability to clot themselves and to interfere with fibrin polymerization.As these fibrinogen degradating enzymes are released by the influence of antigen-antibody-complexes and endotoxine, it can be assumed that clotting defects in patients with acute leukemia, septicemia a. o. are caused by the effects of the proteases on fibrinogen and the accumulation of FDP’s.

The Action of Brinase in Vitro and in Vivo

1975 ◽  
Author(s):  
P. J. Gaffney ◽  
K. Lord ◽  
R. D. Thornes
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Size Range ◽  
Degradation Products ◽  
Molecular Size ◽  
Human Fibrinogen ◽  
Rate Limiting Step ◽  
Rate Limiting

Brinase (an extract of Aspergillus Oryzae) was shown to rapidly digest human fibrinogen in vitro to aggregable degradation products with a molecular size range of 310,000 to 230,000 the latter fragments being more slowly digested to core fragments, Dbr and Ebr. The fibrinogen polypeptide chain susceptibility to Brinase attack was in the order Aα, γ, Bβ, Lysis of the Bβ chain seems to be the rate limiting step in the conversion of the high molecular weight fragments (MW 310,000–230,000) to the core fragments Dbr and Ebr. The conservation of NH2 terminal Tyrosine during fibrinogen digestion and the very transient existence of D dimer fragments during totally crosslinked fibrin lysis suggest that the carboxy end of the γ chain is prone to Brinase attack. The crosslinked α chains of fibrin, while resistant to plasmin, are vigorously digested by Brinase. The plasma of cancer patients being treated with Brinase contained degraded fibrinogen (lacking intact Aα chains) and their aggregates. These aggregates contained some crosslinked γ chains (γ-γ dimers) suggesting that Brinase in vivo exorcises both a lytic and coagulant effect. Thrombin mediated clots in all the plasmas examined contained no crosslinked α chains. Positive plasma ethanol gelation tests can be explained by the presence of the aggregable high molecular weight fragments observed during the in vitro lysis of fibrinogen by Brinase.

Limited Proteolysis of the Purified Aα Chain of Human Fibrinosen by Plasmin

1975 ◽  
Author(s):  
L. Williams ◽  
G. Murano
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Peptide Mapping ◽  
Proteolytic Enzymes ◽  
Degradation Products ◽  
Limited Proteolysis ◽  
Gel Filtration ◽  
Terminal Region ◽  
Low Molecular Weight ◽  
Human Fibrinogen

Based on evidence that a portion of circulating fibrinogen consists of a family of catabolic intermediates formed by proteolytic degradation of the COOH terminal region of Aα chains, we attempted to obtain early degradation products using the purified alkylated Aα chain derivative of human fibrinogen as the substrate and plasmin as the enzyme. Having established optimal conditions, a preparative quantity of material was digested in 0.1 M tris buffer pH = 9.5; time = 4 min; E/S ratio = 1/75 (mole/mole); temp = 37° C. Low molecular weight fragments were separated from the larger species, and further purified by gel filtration on Sephadex G-100. Selected early fragments were analyzed by polycrylamide gel electrophoresis, amino acid composition, peptide mapping and partial N-terminal amino acid sequence. Two of the earliest low molecular weight fragments released by plasmin were derived from the N-terminal region of the Aα chain. Their molecular size was estimated at about 10,000 daltons. One fragment contains fibrinopeptide A; both fragments extend beyond Met-51. Our data indicate that: a) the specificity of plasmin on the purified Aα chain differs from that on intact fibrinogen; or b) proteolytic enzymes other than or in addition to plasmin are responsible for the formation of early catabolic fibrinogen intermediates having a degraded Aα chain.(Supported by USPHS N. I. H. Grant HL 14142.)

A Rapid Determination of the Average Molecular Weight of Rubber in Hevea Latex

1951 ◽  
Vol 24 (2) ◽  
pp. 457-461 ◽  
Author(s):  
W. J. van Essen
Keyword(s):  
Molecular Weight ◽  
Intrinsic Viscosity ◽  
Rapid Determination ◽  
Average Molecular Weight ◽  
Lower Molecular Weight ◽  
Molecular Weights

Abstract A method is described for determining viscometrically the molecular weight of rubber in freshly tapped latex. For this purpose the latex is dissolved in a toluene-pyridine mixture. From the intrinsic viscosity of this solution the molecular weight of the rubber can be determined by the Staudinger equation and a known viscosity constant. Molecular weights varying between 238,000 and 480,000 have been found, depending on the kind of clone. Rubber in fresh latex does not have a lower molecular weight than in old preserved latex.

In Vitro Formation of Fibrin-Monomer Complexes in the Presence of Isotope Labelled Fibrinogen-Fibrin Degradation Products. An Agarose Gel Filtration Study

1975 ◽  
Author(s):  
F. Asbeck ◽  
van de J. Loo
Keyword(s):  
Molecular Weight ◽  
Complex Formation ◽  
Degradation Products ◽  
Gel Filtration ◽  
Agarose Gel ◽  
Fibrinogen Degradation Products ◽  
Molecular Weights ◽  
Fibrin Degradation Products ◽  
Fibrin Monomer

Human citrated plasmas were mixed with purified 131I-fibrinogen and 131I-fibrinogen degradation products (FDP) or 125I-fibrin degradation products (fdp). After incubation with small amounts of thrombin (0.01–0.02 imits/ml Pl.), these mixtures were gel filtrated on Biogel A5m columns and the elution patterns of the 131I- and -labelled materials were determined.In control experiments without thrombin incubation, no complex formation between fibrinogen, FDP or fdp in citrated plasmas could be detected. This was even true for fdp with a higher molecular weight than fibrinogen.After thrombin incubation, up to 11% fibrin-monomer complexes were formed. Irrespective of their molecular weights, labelled fdp were not incorporated into these complexes.Only large FDP – presumably derivative X – did partially copolymerize with fibrin-monomer complexes in citrated plasmas.

Characterization of GTMAC-Graft-Chitosan as a Bactericidal Agent for Nitric Oxide Release

2011 ◽  
Vol 236-238 ◽  
pp. 2967-2972 ◽  
Author(s):  
Yong Liu ◽  
Yan Sun ◽  
Peng Yang ◽  
Yao Xing Xu ◽  
Yan Li Li ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Molecular Weight ◽  
Inhibition Zone ◽  
Lower Molecular Weight ◽  
Water Control ◽  
No Donor ◽  
Nitric Oxide Release ◽  
E Coli ◽  
Molecular Weights ◽  
No Release

This work aims to prepare and characterize one kind of nitric oxide (NO)-releasing conjugation of quaternary ammonium salt to chitosan, as well as to evaluate the anti-bacterial properties of diazeniumdiolates and the changes in NO release properties. The newly synthesized diazeniumdiolates are obtained from glycidyl-trimethyl-ammonium chloride (GTMAC)-bearing chitosan derivatives (HTCC) with different molecular weights (280 and 670 KDa) and are used as NO donor species. An HTCC with high molecular weight (670 KDa) exhibits higher storage capacity for NO (up to 357.70 nmol NO/mg) than one with a low molecular weight (280 kDa). The NO release durations (7 h) observed for the HTCC diazeniumliolates with higher molecular weight (670 kDa) was slightly higher than that of HTCC diazeniumliolates with lower molecular weight (280 kDa). By determining the inhibition zone diameter, HTCC-NO with lower molecular weight (280 kDa) showed significantly higher inhibition capabilities againstE. colithan HTCC, crude chitosan, and water control.

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