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Fibrinopeptides amino acid sequence

Scheme 21 Amino Acid Sequence of a Segment of Fibrinopeptide A and Its p-Turn Peptidomimeticsl%l... Scheme 21 Amino Acid Sequence of a Segment of Fibrinopeptide A and Its p-Turn Peptidomimeticsl%l...
Figure 2.4 Tandem mass spectrum obtained for fibrinopeptide A. A solution of fibrinopeptide A at 33fmol j.L 1 was infused at a flow rate of 200-300nLmin 1 from reservoir 1 using the conditions indicated in Figure 2.3A. The buffer was 10mM acetic acid, pH = 3.0, containing 10% (v/v) methanol. The Y ion series is indicated by full lines. The B ion series is indicated by broken lines. The letters in the right upper corner indicate the fibrinopeptide A amino acid sequence in the one-letter code. (Adapted with permission from Ref. 7). Figure 2.4 Tandem mass spectrum obtained for fibrinopeptide A. A solution of fibrinopeptide A at 33fmol j.L 1 was infused at a flow rate of 200-300nLmin 1 from reservoir 1 using the conditions indicated in Figure 2.3A. The buffer was 10mM acetic acid, pH = 3.0, containing 10% (v/v) methanol. The Y ion series is indicated by full lines. The B ion series is indicated by broken lines. The letters in the right upper corner indicate the fibrinopeptide A amino acid sequence in the one-letter code. (Adapted with permission from Ref. 7).
FIGURE 3.28 Simplified spectrum of y ions showing the amino acid sequence of glutamine fibrinopeptide B. [Pg.165]

Fibrin polymerization is initiated by the enzymatic cleavage of the fibrinopeptides, converting fibrinogen to fibrin monomer (Fig. 1). Then, several nonenzymatic reactions yield an orderly sequence of macromolec-ular assembly steps. Several other plasma proteins bind specifically to the resulting fibrin network. The clot is stabilized by covalent ligation or crosslinking of specific amino acids by a transglutaminase, Factor XHIa. [Pg.263]

Top) peptide ladder sequencing principle. Phenyl isothiocyanate (PITC) produces phenylthiohydantoin (PTH) of the terminal amino acid and a new peptide with one less amino acid. Phenyl isocyanate (PIC), in low quantity, produces N-terminal phenylcarba-mate (PC) from a small fraction of each peptide. (Bottom) example of sequencing of [Glu1]fibrinopeptide B. Reproduced (modified) from Chait B.T., Wang R., Beavis R.C. and Kent S.B.H., Science, 262, 89, 1993, with permission. [Pg.335]

Fibrinopeptides the two pairs of peptides (A and B) cleaved from the /V-termini of the 2a and 2P chains of fibrinogen by thrombin. F. arise by cleavage of Arg-GIy bon so that Arg is the C-terminal end of the F, and Gly is the A/-terminal end of the a and P chains of fibrin. Human FA. is Ala-Asp-Ser-Gly-Glu-Gly-Asp-Phe-Leu-Ala-Glu-(Gly)3-Val-Arg, and human F.B. is Pyr-Glu-Gly-Val-Asn-Asp-Asn-(Glu)2-Gly-(Phe)2-Ser-Ala-Arg. F.A. ranges in size from 14 amino acids (horse, lizard) to 19 (cattle), and F.B. from 9 (rhesus monkeys) to 21 (cattle, elk and kangaroo). The sequences of the F. have been used to establish a detailed phylogenetic tree for mammals which is very similar to the classical one. The F. have a vasoconstrictive effect which serves to keep the coagulation principles from being removed too quickly from an injury site. [Pg.224]


See other pages where Fibrinopeptides amino acid sequence is mentioned: [Pg.124]    [Pg.125]    [Pg.439]    [Pg.268]    [Pg.404]    [Pg.404]    [Pg.11]    [Pg.177]    [Pg.119]    [Pg.445]    [Pg.445]   
See also in sourсe #XX -- [ Pg.144 ]




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