Fibrinopeptide B (human) acetate salt
Fibrinopeptide B (human) acetate salt structure
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Common Name | Fibrinopeptide B (human) acetate salt | ||
|---|---|---|---|---|
| CAS Number | 36204-23-6 | Molecular Weight | 1552.56000 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C66H93N19O25 | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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Novel aspects of fibrin(ogen) fragments during inflammation.
Mol. Med. 17(5-6) , 568-73, (2011) Coagulation is fundamental for the confinement of infection and/or the inflammatory response to a limited area. Under pathological inflammatory conditions such as arthritis, multiple sclerosis or sepsis, an uncontrolled activation of the coagulation system co... |
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Fibrinopeptides A and B release in the process of surface fibrin formation.
Blood 117 , 1700-1706, (2011) Fibrinogen adsorption on a surface results in the modification of its functional characteristics. Our previous studies revealed that fibrinogen adsorbs onto surfaces essentially in 2 different orientations depending on its concentration in the solution: "side... |
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Fibrinogen residue γAla341 is necessary for calcium binding and 'A-a' interactions.
Thromb. Haemost. 107(5) , 875-83, (2012) The fibrinogen γ-module has several important sites relating to fibrinogen function, which include the high affinity calcium binding site, hole 'a' that binds with knob 'A', and the D:D interface. Residue γAla341, which is located in the vicinity of these sit... |
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The application of atmospheric pressure matrix-assisted laser desorption/ionization to the analysis of long-term cryopreserved serum peptidome.
Anal. Biochem. 417(2) , 174-81, (2011) Although most time-of-flight (TOF) mass spectrometers come equipped with vacuum matrix-assisted laser desorption/ionization (MALDI) sources, the atmospheric pressure MALDI (API-MALDI) source is an attractive option because of its ability to be coupled to a wi... |
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Kinetic characterization of inhibition of human thrombin with DNA aptamers by turbidimetric assay.
Anal. Biochem. 421(1) , 234-9, (2012) A sensitive turbidimetric method for detecting fibrin association was used to study the kinetics of fibrinogen hydrolysis with thrombin. The data were complemented by high-performance liquid chromatography (HPLC) measurements of the peptide products, fibrinop... |
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TA-2, a thrombin-like enzyme from the Chinese white-lipped green pitviper (Trimeresurus albolabris): isolation, biochemical and biological characterization.
Blood Coagul. Fibrinolysis 23(5) , 445-53, (2012) Through three chromatographic steps, a new thrombin-like enzyme (TLE), named TA-2, from the venom of the Chinese white-lipped green pitviper (Trimeresurus albolabris) has been isolated and purified to homogeneity. TA-2 was a single-chain glycoprotein with abo... |
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Fibrinogen and fibrin polymerization: appraisal of the binding events that accompany fibrin generation and fibrin clot assembly.
Blood Coag. Fibrinolysis 8 , 257-267, (1997) Fibrinogen is a complex multifunctional protein comprised of three major domains (two outer D and one central E) which contains constitutive binding sites (e.g. Da, Db, gammaXL, D:D, gamma', thrombin substrate, platelet receptor) as well as binding sites that... |
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Substitution of tyrosine for phenylalanine in fibrinopeptide A results in preferential thrombin cleavage of fibrinopeptide B from fibrinogen.
Biochemistry 37 , 13704-13709, (1998) Phenylalanine at residue 8 in the Aalpha chain of fibrinogen is a highly conserved amino acid that is believed to be critical for binding and catalysis by the serine protease thrombin. We have examined the requirement for Phe at this position by constructing ... |
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Role of 'B-b' knob-hole interactions in fibrin binding to adsorbed fibrinogen.
J. Thromb. Haemost. 5(12) , 2344-51, (2007) The formation of a fibrin clot is supported by multiple interactions, including those between polymerization knobs 'A' and 'B' exposed by thrombin cleavage and polymerization holes 'a' and 'b' present in fibrinogen and fibrin. Although structural studies have... |
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Different target surfaces for the analysis of peptides, peptide mixtures and peptide mass fingerprints by AP-MALDI ion trap-mass spectrometry.
J. Proteomics 74(7) , 975-81, (2011) The desorption/ionization behavior of individual peptides, an equimolare peptide mixture and a tryptic digest was investigated by AP-MALDI-IT-MS using four different target materials (gold-covered stainless steel (SS), titanium nitride-covered SS, hand-polish... |