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  1. en.wikipedia.org › wiki › AprotininAprotinin - Wikipedia

    It has a molecular weight of 6512 Da and consists of 16 different amino acid types arranged in a chain 58 residues long [4] [5] that folds into a stable, compact tertiary structure of the 'small SS-rich" type, containing 3 disulfides, a twisted β-hairpin and a C-terminal α-helix.

  2. pubchem.ncbi.nlm.nih.gov › compound › AprotininAprotinin - PubChem

    Aprotinin (40 microg/mL) increased platelet force from 5630 to 11,138+/-562 in PRP devoid of heparin. Aprotinin did not affect thrombin activity, fibrin structure, platelet aggregation or secretion. Aprotinin counteracts heparin suppression of platelet force and enhances platelet force in the absence of heparin.

  3. Aprotinin from bovine lung (Trasylol ); Gel filtration molecular weight marker; Aprotinin is a competitive serine protease inhibitor that forms stable complexes with and blocks the active sites of enzyme;

  4. 12 Φεβ 2009 · Aprotinin is a serine protease inhibitor used to reduce the risk for perioperative blood loss and the need for blood transfusion in high-risk patients during cardiopulmonary bypass for coronary artery bypass graft surgery.

  5. www.sigmaaldrich.com › enzyme-activity-assays › aprotinin-monographAprotinin - MilliporeSigma

    While aprotinin and bovine pancreatic trypsin inhibitor (BPTI) are the same protein sequence, the term aprotinin is typically used when describing the protein derived from bovine lung. Aprotinin is a single peptide chain with three disulfide bonds. Molecular Weight: ~ 6511 1. E1% 280 nm =8.3 (water) pI = 10.5 6.

  6. Molecular Weight: 6511.44. EC Number: 232-994-9. MDL number: MFCD00130541. UNSPSC Code:

  7. 2 ημέρες πριν · Aprotinin is a reversible inhibitor of serine proteases such as trypsin (K i = 0.06 pM), chymotrypsin (K i = 9.5 nM), and kallikrein (K i = 0.8 nM). It is a much weaker inhibitor of thrombin (K i = 0.1-0.8 mM) and trypsinogen (K i = 2 μM). Aprotinin also competitively inhibits nNOS and iNOS with K i values of 50 and 78 μM, respectively ...

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