scholarly journals Using Synthetic Peptide Substrates to MeasureDrosophilaCaspase Activity

2015 ◽  
Vol 2015 (7) ◽  
pp. pdb.prot086231
Author(s):  
Donna Denton ◽  
Sharad Kumar
Keyword(s):  
Synthetic Peptide ◽  
Peptide Substrates

Vitamin K Dependent Carboxylaticn Of Peptide Bound Glutamic Acid Residues

1981 ◽  
Author(s):  
D P Kosow ◽  
M P Esnouf ◽  
A I Gainey ◽  
H A O Hill ◽  
P J Thornally
Keyword(s):  
Carbon Dioxide ◽  
Glutamic Acid ◽  
Rat Liver ◽  
Vitamin K ◽  
Active Carbon ◽  
Synthetic Peptide ◽  
Alcoholic Solution ◽  
Chemical Mechanism ◽  
Peptide Substrates ◽  
Rapid Formation

The chemical mechanism by which vitamin K promotes the posttranslational carboxylation of specific glutamic acid residues in the N-terminal region of prothrombin has not yet been elucidated. We have previously suggested that vitamin K reacts with dioxygen and carbon dioxide to form a species of active carbon. In this study we have investigated the reaction of reduced vitamin K in alcoholic solution with dioxygen in the presence and absence of carbon dioxide. We find that carbon dioxide is necessary for the rapid formation of vitamin K oxide. Vitamin K oxide was formed when either cis or trans vitamin K was used. However, trans vitamin K is specifically required in enzymatic carboxylation studies. We propose that in rat liver microsomal preparations the carboxylation of synthetic peptide substrates is coupled to the chemical epoxidation of vitamin K by the carboxylase.

90 Characterisation of an HCV NS3/NS4A proteinase fusion protein expressed in E.coli using synthetic peptide substrates

1997 ◽  
Vol 25 (4) ◽  
pp. S624-S624 ◽  
Author(s):  
TREVOR C.I. WILKINSON ◽  
PETER R. BUNYARD ◽  
KATHLEEN QUIRK ◽  
CLAIRE S. WILKINSON
Keyword(s):  
Fusion Protein ◽  
Synthetic Peptide ◽  
Peptide Substrates

scholarly journals Reaction of a tumour-associated trypsin inhibitor with serine proteinases associated with coagulation and tumour invasion

1988 ◽  
Vol 254 (3) ◽  
pp. 911-914 ◽  
Author(s):  
U Turpeinen ◽  
E Koivunen ◽  
U H Stenman
Keyword(s):  
Plasminogen Activator ◽  
Tissue Plasminogen Activator ◽  
Trypsin Inhibitor ◽  
Synthetic Peptide ◽  
Serine Proteinases ◽  
Tumour Invasion ◽  
Peptide Substrates ◽  
Tissue Plasminogen

The inhibition of six serine proteinases by a tumour-associated trypsin inhibitor (TATI) was studied using synthetic peptide substrates. Physiological concentrations of TATI inhibited the amidolytic activities of trypsin, plasmin, urokinase and tissue plasminogen activator (tPA). Chymotrypsin, kallikrein and thrombin were also inhibited, but by much higher concentrations of TATI. The ability of TATI to inhibit trypsin, plasmin, urokinase and tPA suggests that it has a role in proteolytic processes in vivo involving these enzymes.

Characterization of Synthetic Peptide Substrates for p34cdc2 Protein Kinase

1991 ◽  
Vol 45 (4) ◽  
pp. 391-400 ◽  
Author(s):  
Daniel R. Marshak ◽  
Mark T. Vandenberg ◽  
Young Seuk Bae ◽  
Ii Je Yu
Keyword(s):  
Protein Kinase ◽  
Synthetic Peptide ◽  
Peptide Substrates

scholarly journals The specificity of some pig and human pepsins towards synthetic peptide substrates

1979 ◽  
Vol 179 (1) ◽  
pp. 247-249 ◽  
Author(s):  
A P Ryle ◽  
C A Auffret
Keyword(s):  
General Formula ◽  
Synthetic Peptide ◽  
Peptide Substrates ◽  
Alanine Residue ◽  
Leucine Residue ◽  
Rate Of Hydrolysis

1. The peptidase activities of pig pepsins A and C and human pepsin and gastricsin were compared. 2. The peptides studied had the general formula A Leu Val-His-B. Hydrolysis at 37 degrees C and pH 2.07 occurred at the amino side of the leucine residue for all the enzymes and all the peptides. 3. When A was Ac-Ala the peptides were hydrolysed under these conditions slowly by pig pepsin C only. 4. Pig pepsin A and human pepsin were unable to hydrolyse the tyrosine-containing peptides under the conditions tested. Gastricsin (human pepsin C) had about one-third of the activity of pig pepsin C with these substrates. 5. The increase in the rate of hydrolysis caused by the extension of the chain by a single alanine residue was most marked for pig pepsin A and human pepsin.

Synthetic Peptide Assays For Monitoring The Defects Of Extrinsic And Intrinsic Pathways Of Coagulation: Selection Of A Suitable Substrate

1981 ◽  
Author(s):  
Jeanine Walenga ◽  
Jawed Fareed ◽  
Harry L Messmore ◽  
Judith Kniffin
Keyword(s):  
Partial Thromboplastin Time ◽  
Synthetic Peptide ◽  
Serine Proteases ◽  
Developmental Stages ◽  
Peptide Substrate ◽  
Amidolytic Activity ◽  
Proper Selection ◽  
Peptide Substrates ◽  
Free Peptide ◽  
Selection Of

Several assays based on the use of thrombin specific synthetic peptide substrates have been proposed for the amidolytic equivalents of prothrombin time (PT) and partial thromboplastin time (PTT). All of these methods employ the same principle as the clotting assays; the test plasma is activated with either thromboplastin or activator-cephalo-plastin mixture and the generated thrombin activity is measured employing thrombinr specific synthetic substrates such as Bz-Phe-Val-Arg-pNA (S-2160), H-D-Phe-Pip-Arg-pNA (S-2238), Tos-Gly-Pro-Arg-pNA (Chromozym TH), and CH3-Gly- Pro-Arg-pNA. These substrates and their free peptide forms inhibit the amidolytic action of bovine Xa activated human and Xa Russell’s viper venom in the following order: S-2160 > S-2238 > Sarc-Pro-Arg-pNA ≥ Chromozym TH. A new substrate for thrombin Pyro-Glu-Pro-Arg-pNA (S-2366) and a plasminogen activator (tissue) substrate, H-D-Ile-Pro-Arg-pNA (S-2288) have been tested and were found to produce weaker inhibition of bovine and human Xa. Tos-Gly-Pro-Arg-pNA, Sarc-Pro-Arg-pNA and H-D-Ile-Pro-Arg-pNA were found to produce a ≤ 10% inhibition of the activator generated Xa’s amidolytic activity at concentrations which are commonly employed in the PT and PTT assays. Although in the developmental stages the synthetic substrate equivalent assays are more sensitive than the existing PT and PTT assays and provide useful information on the total amount of thrombin generated in each assay, our results suggest that amidolytic equivalent assays for PT and PTT are feasable. However proper selection of a peptide substrate is important as some of the thrombin substrates and their free peptide forms may inhibit Xa and other serine proteases which are generated during the activation step thereby seriously influencing the results.

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