scholarly journals Specific peptide-bond cleavage by microwave irradiation in weak acid solution

1992 ◽  
Vol 11 (1) ◽  
pp. 45-50 ◽  
Author(s):  
Chi-Yue Wu ◽  
Shui-Tein Chen ◽  
Shyh-Horng Chiou ◽  
Kung-Tsung Wang
Keyword(s):  
Microwave Irradiation ◽  
Acid Solution ◽  
Bond Cleavage ◽  
Peptide Bond ◽  
Weak Acid ◽  
Peptide Bond Cleavage ◽  
Specific Peptide

scholarly journals Myxobacter AL-1 Protease II: Specific Peptide Bond Cleavage on the Amino Side of Lysine

1972 ◽  
Vol 112 (2) ◽  
pp. 940-949 ◽  
Author(s):  
Marilyn Wingard ◽  
Gary Matsueda ◽  
R. S. Wolfe
Keyword(s):  
Bond Cleavage ◽  
Peptide Bond ◽  
Peptide Bond Cleavage ◽  
Specific Peptide

Formation of substituted 1-Benzazepine-2,5-diones from derivatives of kynurenine

1978 ◽  
Vol 31 (2) ◽  
pp. 439 ◽  
Author(s):  
DE Rivett ◽  
FHC Stewart
Keyword(s):  
Bond Cleavage ◽  
Peptide Bond ◽  
Thermal Cyclization ◽  
Model Compounds ◽  
Peptide Bond Cleavage ◽  
Derivatives Of ◽  
Substituted 1 ◽  
Specific Peptide

Several N-protected DL-kynurenine derivatives have been converted into 3-substituted 3,4-dihydro-1H-1-benzazepine-2,5-diones by thermal cyclization. This reaction was found to proceed less readily than the analogous formation of 1,4-benzodiazepine-2,5-diones from o- aminobenzoylamino acids. The incidence of specific peptide bond cleavage involving these cyclizations was investigated with model compounds.

scholarly journals Serine protease dynamics revealed by NMR analysis of the thrombin-thrombomodulin complex

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Riley B. Peacock ◽  
Taylor McGrann ◽  
Marco Tonelli ◽  
Elizabeth A. Komives
Keyword(s):  
Active Site ◽  
Serine Proteases ◽  
Protein C ◽  
Catalytic Mechanism ◽  
Bond Cleavage ◽  
Peptide Bond ◽  
Peptide Bond Cleavage ◽  
Exchange Mass Spectrometry ◽  
Catalytically Active ◽  
Hydrogen Deuterium

AbstractSerine proteases catalyze a multi-step covalent catalytic mechanism of peptide bond cleavage. It has long been assumed that serine proteases including thrombin carry-out catalysis without significant conformational rearrangement of their stable two-β-barrel structure. We present nuclear magnetic resonance (NMR) and hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments on the thrombin-thrombomodulin (TM) complex. Thrombin promotes procoagulative fibrinogen cleavage when fibrinogen engages both the anion binding exosite 1 (ABE1) and the active site. It is thought that TM promotes cleavage of protein C by engaging ABE1 in a similar manner as fibrinogen. Thus, the thrombin-TM complex may represent the catalytically active, ABE1-engaged thrombin. Compared to apo- and active site inhibited-thrombin, we show that thrombin-TM has reduced μs-ms dynamics in the substrate binding (S1) pocket consistent with its known acceleration of protein C binding. Thrombin-TM has increased μs-ms dynamics in a β-strand connecting the TM binding site to the catalytic aspartate. Finally, thrombin-TM had doublet peaks indicative of dynamics that are slow on the NMR timescale in residues along the interface between the two β-barrels. Such dynamics may be responsible for facilitating the N-terminal product release and water molecule entry that are required for hydrolysis of the acyl-enzyme intermediate.

Activation of Bovine Factor V by Thrombin and A Protease From Russell's Viper Venom (RVV)

1979 ◽  
Author(s):  
M.J. Lindhout ◽  
C. M. Jackson
Keyword(s):  
Bond Cleavage ◽  
Peptide Bond ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Factor V ◽  
Peptide Bond Cleavage ◽  
Prothrombinase Complex ◽  
Factor Va ◽  
Activation Products ◽  
Ca Oxalate

In order to understand the function of activated factor V in the prothrombinase complex, we isolated the activation products obtained by action of thrombin and RVV-V on factor V and studied their functional properties. Factor V isolated from plasma by means of ion-exchange chromatography, a Ca-oxalate adsorption step and gelfiltration was homogenous in SDS-gelelectrophoresis (apparent MW 360,000, with and without reduction). Increase in factor V activity upon action by RVV-V is correlated with a single peptide bond cleavage, resulting in a 270,000 dalton and a 80,000 dalton component. Additional proteolysis of factor Va(RVV/V)’ by thrombin results in a further cleavage of the high MW component into peptides with MW's of 72,000, 94,000 and about 150,000 without a furth~r increase in factor V activity. Whereas none of the isolated peptides reveal factor Va activity, activity would be generated by a recombination in the presence of Ca2+ of the 94,000 MW or 270,000 MW component with the 80,000 component. Action of thrombin alone on factor V results in peptides of MW 72,000, 80,000, 94,000 and a peptide very rich in carbohydrate with an apparent MW of 150,000.

Demasking kinetics of peptide bond cleavage for whey protein isolate hydrolysed by Bacillus licheniformis protease

2016 ◽  
Vol 133 ◽  
pp. S426-S431 ◽  
Author(s):  
Mikhail M. Vorob’ev ◽  
Claire I. Butré ◽  
Stefano Sforza ◽  
Peter A. Wierenga ◽  
Harry Gruppen
Keyword(s):  
Whey Protein ◽  
Bacillus Licheniformis ◽  
Bond Cleavage ◽  
Peptide Bond ◽  
Whey Protein Isolate ◽  
Protein Isolate ◽  
Peptide Bond Cleavage ◽  
Kinetics Of
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