Inhibition of Platelet Aggregation by Dialysable Fibrinogen Degradation Products (FDP)

1970 ◽  
Vol 23 (01) ◽  
pp. 091-098 ◽  
Author(s):  
Jolanta Stachurska ◽  
Z Latałło ◽  
Maria Kopeć
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Platelet Aggregation ◽  
Active Component ◽  
Degradation Products ◽  
Aromatic Amino Acids ◽  
Inhibit Platelet Aggregation ◽  
Molecular Fragments ◽  
Fibrinogen Degradation Products ◽  
Inhibition Of Platelet Aggregation

SummaryDuring prolonged proteolysis of fibrinogen by plasmin dialysable, low molecular fragments accumulate which inhibit platelet aggregation induced by thrombin, ADP, adrenaline and noradrenaline. These fragments isolated by dialysis were separated on sephadex G-25 column. The active component has probably a molecular weight lower than 5,000 and does not contain aromatic amino acids.

Some Effects of Fibrinogen Degradation Products (FDP) on Blood Platelets

1966 ◽  
Vol 15 (03/04) ◽  
pp. 413-419 ◽  
Author(s):  
Z Jerushalmy ◽  
M. B Zucker
Keyword(s):  
Platelet Aggregation ◽  
Connective Tissue ◽  
Degradation Products ◽  
Blood Platelets ◽  
Adenosine Diphosphate ◽  
Serotonin Release ◽  
Fibrinogen Degradation Products ◽  
Inhibition Of Platelet Aggregation

Summary“Early” fibrinogen degradation products are more potent inhibitors of thrombin-induced clotting than “late” products and also interfere with the ability of thrombin to release serotonin from platelets. “Early” and “intermediate” FDP cause moderate inhibition of platelet aggregation induced by adenosine diphosphate or connective tissue particles. Serotonin release by connective tissue particles is probably not inhibited by FDP.

Inhibitory Effect of Staphylokinase on Platelet Aggregation

1993 ◽  
Vol 70 (05) ◽  
pp. 834-837 ◽  
Author(s):  
Akira Suehiro ◽  
Yoshio Oura ◽  
Motoo Ueda ◽  
Eizo Kakishita
Keyword(s):  
Platelet Aggregation ◽  
Human Platelet ◽  
Degradation Products ◽  
Platelet Rich Plasma ◽  
Inhibitory Effect ◽  
Effective Concentration ◽  
Inhibit Platelet Aggregation ◽  
Platelet Suspension ◽  
Washed Platelet ◽  
Human Platelet Aggregation

SummaryWe investigated the effect of staphylokinase (SAK), which has specific thrombolytic properties, on human platelet aggregation. Platelet aggregation induced with collagen was observed following preincubation of platelets in platelet-rich plasma (PRP) or washed platelet suspension (WP) with SAK at 37° C for 30 min. SAK inhibited platelet aggregation in PRP only at the highest examined concentration (1 x 10-4 g/ml). Although SAK did not inhibit platelet aggregation in WP which contained fibrinogen, it did when the platelets had been preincubated with SAK and plasminogen. The most effective concentration in WP was 1 x 10-6 g/ml. The effect could be inhibited by adding aprotinin or α2-antiplasmin. The highest generation of plasmin in the same preincubation fluid was detected at 1 x 10-6 g/ml SAK. We concluded that SAK can inhibit platelet aggregation in WP by generating plasmin and/or fibrinogen degradation products, but is only partially effective in PRP because of the existence of α2-antiplasmin.

Characterization of an isozyme of S-adenosylmethionine synthetase from rat liver

1984 ◽  
Vol 62 (5) ◽  
pp. 276-279 ◽  
Author(s):  
C. H. Lin ◽  
W. Chung ◽  
K. P. Strickland ◽  
A. J. Hudson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Enzymatic Synthesis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Aromatic Amino Acids ◽  
Adenosylmethionine Synthetase ◽  
Cellulose Column

An isozyme of S-adenosylmethionine synthetase has been purified to homogeneity by ammonium sulfate fractionation, DEAE-cellulose column chromatography, and gel filtration on a Sephadex G-200 column. The purified enzyme is very unstable and has a molecular weight of 120 000 consisting of two identical subunits. Amino acid analysis on the purified enzyme showed glycine, glutamate, and aspartate to be the most abundant and the aromatic amino acids to be the least abundant. It possesses tripolyphosphatase activity which can be stimulated five to six times by S-adenosylmethionine (20–40 μM). The findings support the conclusion that an enzyme-bound tripolyphosphate is an obligatory intermediate in the enzymatic synthesis of S-adenosylmethionine from ATP and methionine.

Calcium-binding proteins in a vorticellid contractile organelle

1975 ◽  
Vol 19 (1) ◽  
pp. 203-213
Author(s):  
W.B. Amos ◽  
L.M. Routledge ◽  
F.F. Yew
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Sodium Dodecyl ◽  
Aromatic Amino Acids ◽  
Calcium Binding Proteins ◽  
Polyacrylamide Gels ◽  
Protein Species ◽  
Low Concentrations

The proteins of the contractile spasmoneme of Zoothamnium have been examined for comparison with other motile systems. Though capable of calcium-induced contraction, glycerinated preparations of the spasmoneme contain neither actin nor tubulin at levels that can be detected in polyacrylamide gels. Sixty per cent of the protein in sodium dodecyl sulphate gels migrates in a band at a molecular weight of approximately 20,000, consisting largely of 2 similar protein species which are here given the name of spasmins. The amino acid composition of 2 spasmin fractions has been determined by a fluorimetric method. They are rich in Asx, Glx and serine, but have few aromatic amino acids and no cystine or methionine. In calcium-buffered polyacrylamide gels, it was observed that a reduction in the electrophoretic mobility of the spasmins was induced specifically by calcium (but not magnesium) at the same low concentrations as induce contraction. This indicates that the spasmins are calcium-binding proteins which may be involved directly in the calcium-induced contraction of the spasmoneme.

Low Molecular Weight Sunflower Protein Hydrolysate with Low Concentration in Aromatic Amino Acids

1996 ◽  
Vol 44 (4) ◽  
pp. 967-971 ◽  
Author(s):  
Juan Bautista ◽  
Inmaculada Hernandez-Pinzon ◽  
Manuel Alaiz ◽  
Juan Parrado ◽  
Francisco Millan
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Protein Hydrolysate ◽  
Aromatic Amino Acids ◽  
Low Molecular Weight ◽  
Low Concentration ◽  
Sunflower Protein

scholarly journals Products of Metabolism and Processing of Lactic Acid Bacteria as Functional Ingredients

2018 ◽  
Vol 1 (1) ◽  
pp. 47 ◽  
Author(s):  
Antonina Ivanovna Kapustian ◽  
Natalia Cherno ◽  
Alexei Kovalenko ◽  
Kristina Naumenko ◽  
Igor Kushnir
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
Organic Acids ◽  
Cell Walls ◽  
Degradation Products ◽  
Lactobacillus Delbrueckii ◽  
Low Molecular Weight ◽  
Gel Chromatography

Lactic acid bacteria (LAB) and bifidobacteria (BB) are unique substances that have a lot of biological and physiological effects. Structural components of LAB and BB – peptidoglycans, compounds of the muramylpeptide series, teichoic acids – have powerful immunological properties. Metabolites of LAB and BB – organic acids, hydrogen peroxide, bacteriocins, etc. – provide antagonistic activity, have an indirect impact on the immune system, reducing the antigenic load caused by pathogenic microorganisms. The expediency of peptidoglycans degradation of LAB and BB cell walls is substantiated. Low molecular weight products of the degradation can easily be absorbed and enter into biochemical processes, accelerating the expected functional-physiological effect. To obtain low-molecular products of peptidoglycans degradation, a combination of LAB and BB was used. The combination of LAB and BB is the sum of the test cultures of Lactobacillus acidophilus, Lactobacillus delbrueckii subsp. Bulgaricus, Bifidobacterium bifidum, Lactococcus cremoris, Streptococcus termophilus. Destruction of peptidoglycans of bacterial cell walls was carried out using a combination of disintegrating factors. The efficiency of destruction was determined by the accumulation of low molecular weight peptides (with molecular weight up to 1500 Da), amino acids and soluble protein in the disintegrate. It has been established that the highest accumulation of low molecular weight degradation products occurs when using autolysis followed by enzymatic hydrolysis during 180 min with the ratio of the enzyme : substrate 1 : 100. At the same time ≈ 53% of protein substances pass from insoluble to soluble state. The molecular weight of the obtained products is determined by the gel chromatography method. The qualitative and quantitative content of organic acids, amino acids and vitamins of group В in the hydrolysis products composition was investigated. It was shown that the obtained product possesses high biological effect in the experiment on animals.

Kinin-like Activities of the Synthetic Low Molecular Weight Fragment of Fibrinogen Degradation Products

1974 ◽  
Vol 32 (02/03) ◽  
pp. 350-355
Author(s):  
Akira Takaki ◽  
Tsuyoshi Yamaguchi ◽  
Keiichi Ohsato
Keyword(s):  
Molecular Weight ◽  
Smooth Muscle ◽  
Muscle Contraction ◽  
Synthetic Peptide ◽  
Degradation Products ◽  
Hypotensive Effect ◽  
Smooth Muscle Contraction ◽  
Biological Properties ◽  
Low Molecular Weight ◽  
Fibrinogen Degradation Products

SummarySome biological properties of a synthetic peptide based on an anticoagulant peptide obtained from fibrinogen degradation products by the action of plasmin are reported. This peptide produced smooth muscle contraction without the presence of bradykinin. The contraction caused by this peptide was not modified by atropin (10-6 g/ml), hyoscine (10-6 g/ml) and tetrodotoxin (2xl0-7 g/ml). A hypotensive effect was observed following the intravenous injection of the peptide into an anesthetized rat indicating that this peptide has an action similar to that of bradykinin though less potent.

Studies on the Role of Fibrinolysis and Fibrinogen Degradation Products (FDP) in Analgesic Action of Morphine

1972 ◽  
Vol 28 (03) ◽  
pp. 359-366 ◽  
Author(s):  
Włodzimierz Buczko ◽  
Konstanty Wiśniewski
Keyword(s):  
Molecular Weight ◽  
Brain Tissue ◽  
Clinical Effect ◽  
Degradation Products ◽  
Analgesic Action ◽  
Fibrinogen Degradation Products ◽  
The Brain

SummaryThe role of fibrinolysis and FDP in the analgesic action of morphine in mice and rats was studied. It was shown that during activation of blood fibrinolysis, both the accumulation of morphine in the brain tissue of rats and the clinical effect of this drug were increased. Similar results were observed after morphine given simultaneously with FDP obtained in vitro. The data from the analysis of FDP carried out on Sephadex G-25 Fine columns suggest that only FDP of molecular weight of about 10,000 potentiate the action of morphine; smaller peptides decreased the action of this drug.

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