ライフサイエンスコーパス: fibrinopeptide A

1 ogen, respectively, batroxobin only releases fibrinopeptide A.

2 rmation seen in both factor XIII-(28-37) and fibrinopeptide A.

3 ion, ITS accumulation, and the production of fibrinopeptide A.

4 cificity constant 280-fold lower than normal fibrinopeptide A.

5 -terminal neoepitope generated by release of fibrinopeptide A.

6 rhauser effect spectroscopy studies of bound fibrinopeptide A(1-16 Ser3P) indicate that phosphorylati

7 n for urothelial carcinoma was identified as fibrinopeptide A-a known biomarker of ovarian cancer and

8 (NaCl, ChCl, or NaF) and is -1.5 +/- 0.1 for fibrinopeptide A and -2.5 +/- 0.1 for fibrinopeptide B.

9 In contrast to thrombin, which releases fibrinopeptide A and B from the NH2-terminal domains of

10 Fibrinogen Longmont had normal fibrinopeptide A and B release and a functional polymeri

11 wo sets of two consecutive Glu residues, and fibrinopeptide A and fibrinopeptide B, with isolated aci

12 h fibrinogen promotes sequential cleavage of fibrinopeptides A and B (fpA and fpB, respectively) from

13 Upon addition of thrombin, fibrinopeptides A and B are cleaved off from the N-termi

14 The release of fibrinopeptides A and B by the slow and fast forms of th

15 blood coagulation cascade, thrombin cleaves fibrinopeptides A and B from fibrinogen revealing sites

16 Thrombin cleaves fibrinopeptides A and B from the N-termini of the fibrin

17 -termini of Bbeta chains and that removal of fibrinopeptides A and B upon fibrin assembly results in

18 We found that the release of fibrinopeptides A and B was the same for these variants

19 haC-connector, bound to NDSK, which contains fibrinopeptides A and B, and less frequently to desA-NDS

20 of the alpha- and beta-chains, including the fibrinopeptides A and B, are also disordered.

21 ents of the alpha and beta chains, including fibrinopeptides A and B, are not visible in electron den

22 aining was detected using antibodies against fibrinopeptides A and B, as well as with the T2G1 monocl

23 ogen and fibrin I, leading to the release of fibrinopeptides A and B, is driven by electrostatic forc

24 -knobs, which are exposed by the cleavage of fibrinopeptides A and B, respectively, and between corre

25 late the two knobs exposed by the removal of fibrinopeptides A and B, respectively.

26 g to the knobs exposed by the release of the fibrinopeptides A and B.

27 rd peptides such as YGGFLR, angiotensin III, fibrinopeptide A, and des-Arg1-bradykinin were dissociat

28 ivated factor XII, prothrombin fragment 1+2, fibrinopeptide A, and fibrinogen were measured in 1153 m

29 duced rates for TAT formation but equivalent fibrinopeptide A, and fV activation/inactivation.

30 peptide F1.2, thrombin-antithrombin complex, fibrinopeptide A, and soluble fibrin, combined with a co

31 thrombin-catalyzed fibrinogen activation to fibrinopeptide A are most consistent with a two-proton b

32 T was polymerized with Ancrod, which cleaves fibrinopeptide A at the same rate from either fibrinogen

33 34Val peptide was released more slowly than fibrinopeptide A but more quickly than fibrinopeptide B

34 tor VII, prothrombin fragment 1 + 2, urinary fibrinopeptide A, C-reactive protein, and interleukin-6

35 (2) Fibrinopeptide A cleavage further unmasks the NH2 and Ar

36 this structure with the crystal structure of fibrinopeptide A complexed with thrombin highlights seve

37 eparin reduced beta-thromboglobulin release; fibrinopeptide A concentrations were significantly highe

38 rminal portion (1ADSGE5) of unphosphorylated fibrinopeptide A does not interact with the surface of b

39 We found that the variant fibrinopeptide A (F8Y 1-16) was cleaved by thrombin, in

40 ta-4 (Tbeta-4), fibrinopeptide B (FP-B), and fibrinopeptide A (FP-A).

41 T), prothrombin fragment 1 + 2 (F1 + 2), and fibrinopeptide A (FPA) as well as markers of fibrinolysi

42 ction of which requires different extents of fibrinopeptide A (FpA) cleavage from fibrinogen.

43 were obtained from 247 patients and urinary fibrinopeptide A (FPA) from 178 of the 247.

44 he thrombin-catalyzed cleavage of N-terminal fibrinopeptide A (FPA) from the two Aalpha-chains of fib

45 During cleavage of fibrinogen by thrombin, fibrinopeptide A (FpA) release precedes fibrinopeptide B

46 n platelet activation, formation of TAT, and fibrinopeptide A (FPA) release.

47 amples by immunoassay and immunoblotting for fibrinopeptide A (FPA), thrombin-antithrombin (TAT), fac

48 In addition, fibrinopeptide A (FPA), thrombin-antithrombin III (TAT)

49 plasma levels (at 0, 4, 12, and 24 hours) of fibrinopeptide A (FPA), which reflects thrombin action,

50 vo to fibrinogen and conducting an assay for fibrinopeptide A (FPA).

51 Respective values for plasma fibrinopeptide A (FPA, nmol/L) were 1.52, 1.35, and 1.15

52 depends on the release of the two N-terminal fibrinopeptides A (FPA) from fibrinogen, and its formati

53 ragment of GPIb alpha reduced the release of fibrinopeptide A from fibrinogen by about 50% by a nonco

54 The k(cat)/K(m) for the release of fibrinopeptide A from fibrinogen was 4.5 +/- 0.5 microM(

55 Thrombin failed to release fibrinopeptide-A from fibrinogen(AEK) and failed to indu

56 Fibrinopeptide A generation showed threshold variability

57 vated partial thromboplastin time assays and fibrinopeptide A generation tests.

58 uch as argatroban, were the observation that fibrinopeptide A had antithrombotic properties and deter

59 he hypothesis given above, and indicate that fibrinopeptide A is also involved.

60 ized A'beta fibrinogen, replacing FpB with a fibrinopeptide A-like peptide, FpA' (G14V).

61 Here we present SID of leucine enkephalin, fibrinopeptide A, melittin, insulin chain-B, and a nonco

62 Neither treatment changed fibrinopeptide A or prothrombin fragment 1 and 2.

63 ges were observed with treatment in d-dimer, fibrinopeptide A, prothrombin fragment F1.2, factor VIIa

64 The rate of fibrinopeptide A release was decreased 27-fold, and the

65 Fibrinopeptide A release was normal, whereas fibrinopept

66 Fibrinopeptide A release was slower over the course of t

67 o its higher affinity interaction, selective fibrinopeptide A release, and prothrombotic properties.

68 n concentrations that equalized the rates of fibrinopeptide A release, BbetaA68T fibrinogen polymeriz

69 hrombin activation and fibrin formation with fibrinopeptide A release.

70 eu peptide was released at a similar rate as fibrinopeptide A, the 34Val peptide was released more sl

71 The systemic levels of fibrinopeptide A, thrombin-antithrombin complex, D-dimer

72 Ancrod-induced cleavage of fibrinopeptide A was not affected.

73 le the rate of thrombin-catalyzed release of fibrinopeptide A was similar, the release of fibrinopept

74 exposed by the thrombin-catalyzed removal of fibrinopeptide A, was found to reside in the gamma-chain