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Wednesday, May 6, 2020 | History

2 edition of kinetic study of the action of bovine thrombin and human plasmin on synthetic substrates. found in the catalog.

kinetic study of the action of bovine thrombin and human plasmin on synthetic substrates.

John Brian Baird

kinetic study of the action of bovine thrombin and human plasmin on synthetic substrates.

by John Brian Baird

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Published .
Written in English


Edition Notes

Thesis (Ph. D.)--The Queen"s University of Belfast, 1968.

The Physical Object
Pagination1 v
ID Numbers
Open LibraryOL19928136M

To the Editor-in-Chief: Topical bovine thrombin is commonly used for surgical hemostasis. In the s, it was recognized that patients commonly made antibodies to bovine thrombin following exposure to these agents. 1,2 These antibodies did not cross-react with human thrombin in most cases. However, it soon became apparent that the antibody responses to bovine thrombin could lead to immune. Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human Lysplasmin. Journal of Molecular Biology , (2), DOI: /(86) Paolo Ascenzi, Antonio Torroni, Enea Menegatti, Mario Guarneri, Gino Amiconi. Catalytic properties of human Lysplasmin.

Plasmin is a protease in milk, which concentration is increased during mastitis. The aim of the study was design and characterize short, tailor made fluorogenic substrates for plasmin to see.   Doria C, Fischer CP, Wood CG, Li PM, Marra S, Hart J. Phase 3, randomized, double-blind study of plasma-derived human thrombin versus bovine thrombin in achieving hemostasis in patients undergoing surgery. Curr Med Res Opin. Mar;24(3) doi: /X Epub Jan

Plasmin is a much more promiscuous enzyme than thrombin, but studies using phage display and peptide substrates have revealed that plasmin recognizes substrates resembling the site in . Thrombin also possesses the ability to hydrolyze a variety of ester and amide substrates, but, at least in the case of ester substrates, these synthetic substrates do not effectively measure.


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Kinetic study of the action of bovine thrombin and human plasmin on synthetic substrates by John Brian Baird Download PDF EPUB FB2

Mechanism of action of thrombin on fibrinogen. Kinetic evidence for involvement of aspartic acid at position P Biochemistry22 (18), DOI: /bia Paul A. Janmey, Lorne Erdile, Marsha D. Bale, and John D.

Ferry. In a study of the action of thrombin on fibrinogen and a comparison of this enzyme with trypsin, several fibrinogen-like oligopeptides were synthesized. The hydrolysis of the arginyl-glycine bond in these peptides, by both of these enzymes, is examined and by: Our understanding of the various biological roles of thrombin has been facilitated by the development of convenient chromogenic and fluorogenic assays for the measurement of thrombin activity; and synthetic, low-molecular-weight inhibitors which are important probes for the study of thrombin’s mechanism, specificity, and function in the coagulation by: Reaction mechanisms In overall terms the hydrolytic action of thrombin on synthetic substrates of the ester, thioester or amide type are quite similar.

Cleavage of the carbon- oxygen, the carbon-sulphur or carbon-nitrogen bonds leads to release from the substrate of an alcohol, a Cited by: The kinetic behaviour of human thrombin has been studied with 26 tripeptidyl‐p ‐nitroanilide substrates protected at the N terminus and with 9 unprotected the regression analysis of experimcntally determined 1/K m, k cat, and k cat /K m values the individual contribution of each side chain of the various substrates to the kinetic parameters was by: By using the turbidimetrical procedure, the inhibition constants, Kip, of competitive inhibitors of thrombin were estimated in systems of fibrinogen.

Since thrombin in its action on fibrinogen cleaves an amide linkage, we have devised amide substrates for thrombin. The cleavage of such substrates should reflect the biological function of thrombin better than the cleavage of ester substrates.

Kinetics on the initial reaction of the fibrinogen-fibrin conversion catalyzed by thrombin was studied by turbidimetrical measurement. The turbidity c.

Comparison of structures of various human fibrinogens and a derivative thereof by a study of the kinetics of release of fibrinopeptides. Biochemistry23 (20), DOI: /bia Irvine Lian Hao Ong, Kun-Lin Yang. synthetic substrates.6 Under certain storage conditions, autolytic digestion of -thrombin results in formation of and -thrombins, which lack fibrinolytic activity, but retain some activity against synthetic peptide substrates and protein substrates other than fibrinogen.9 This thrombin preparation is predominantly -thrombin.

The kinetic properties of the esterase action of trypsin thrombin, and plasmin on the ethyl and p-nitropheny esters of p′-guanidinobenzoic acid have been characterized.

Interaction of human protein Z with thrombin: Evaluation of the species difference in the interaction between bovine and human protein Z and thrombin. Biochemical and Biophysical Research Communications(3), DOI: /X(91) M.J.

Weinstein, and R.F. Doolittle, Differential specificities of thrombin, plasmin and trypsin with regard to synthetic and natural substrates and inhibitors, Biochim. Biophys.

Acta. Table 1 Kinetic constants for plasmin and thrombin on single AMC substrates. Full size table Structural determinants of P4-lysine and P2-aromatic substrate specificity in plasmin. Search results for bovine thrombin at Sigma-Aldrich. Abstract. Plasminogen, the zymogen precursor of plasmin, can be separated from mammalian plasmas, serums, and enriched plasma fractions (e.g., fractions III and III 2,3) by an affinity chromatography method with either L-lysine-substituted-Sepharose (Deutsch and Mertz, ; Robbins and Summaria, ) or Polyacrylamide (Rickli and Cuendet, ), and either p-aminobenzamidine-substituted.

Bovine α-Thrombin purity is >95% by SDS-PAGE. This activated enzyme has a minimum activity of 1, NIH units/mg when compared to NIH standard human thrombin. Buffer composition = 50 mM Sodium Citrate/ M NaCl/% PEG/pH Mechanism of action.

In the blood coagulation pathway, thrombin acts to convert factor XI to XIa, VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa. Factor XIIIa is a transglutaminase that catalyzes the formation of covalent bonds between lysine and glutamine residues in fibrin.

The covalent bonds increase the stability of the fibrin clot. the action of thrombin on other substrates as cu-N-toluene- sulfonyl-L-arginine methyl ester and fibrinogen. No change in the molecular size of any of these three forms was detected after exposure to thrombin.

Factor V derived from serum by endogenous thrombin action appeared to have. Thrombin is a two chain enzyme composed of an NH2-terminal "A" chain (Mr=6,) and a COOH-terminal "B" chain (Mr=31,) which remain covalently associated through a single disulfide bond.

Human thrombin is 13 amino acids shorter than the bovine thrombin due to a thrombin cleavage site on the human protein that is not present in the bovine. Effect of thrombomodulin on the kinetics of the interaction of thrombin with substrates and inhibitors.

A rapid method for the purification of bovine thrombin and the inhibition of the purified enzyme wtih phenylmethylsulfonyl fluoride. Rosenberg RD, Damus PS. The purification and mechanism of action of human antithrombin-heparin.Plasmin is created when plasminogen, its precursor, is released into the circulation and activated by tissue plasminogen activator (TPA), urokinase plasminogen activator (uPA), or streptokinase.

The activity of plasmin can be inhibited by the presence of alpha 2-antiplasmin, a serine protease inhibitor.Prepared from freshly collected bovine plasma, bovine Prothrombin is a glycoprotein of molecular wei and consists of a single polypeptide chain.

Activation of Prothrombin by the prothrombinase complex (FXa, FVa, PL and Ca++) yields the serine protease Thrombin.