Some Enzymatic Properties of Trypsin after Reaction with 1-Dimethylaminonaphthalene-5-sulfonyl Chloride

1971 ◽  
Vol 49 (5) ◽  
pp. 516-521 ◽  
Author(s):  
James G. Franklin ◽  
James Leslie
Keyword(s):  
Enzymatic Activity ◽  
Ethyl Ester ◽  
Sulfonyl Chloride ◽  
Lysine Residue ◽  
Enzymatic Properties ◽  
Tyrosine Residue ◽  
General Increase ◽  
Enhanced Activity

At pH 7–8, and at 0–25°, 1-dimethylaminonaphthalene-5-sulfonyl chloride reacts with an isoleucine and a lysine residue, with some additional reaction at a tyrosine residue, in trypsin. The enzymatic activity of the modified trypsin toward N-benzoyl-DL-arginme p-nitroanilide is greater than that of the unmodified enzyme, but there is little or no change in activity toward N-benzoyl-L-arginine ethyl ester, N-benzoyl-DL-arginine ethyl ester, and N-benzoyl-L-arginine amide. The enhanced activity does not appear to be due to a general increase in the catalytic part of the mechanism of trypsin action, but rather to an increased binding of N-benzoyl-L-argimne p-nitroanilide to the enzyme.

scholarly journals Studies on separation and properties of lumbrokinase in Pheretima praepinguis

2016 ◽  
Vol 11 ◽  
pp. S106-S109
Author(s):  
Tang Mei ◽  
Liu Cao ◽  
Liang Zi ◽  
Gong Mingfu ◽  
Hu Die
Keyword(s):  
High Temperature ◽  
Enzymatic Activity ◽  
Enzymatic Properties ◽  
Temperature Adaptation ◽  
Plate Method ◽  
Salting Out ◽  
Effect Of Ph ◽  
Alkaline Environment ◽  
Method Effect ◽  
Wide Range

The purpose of this study was to separate lumbrokinase in Pheretima praepinguis and examine its enzymatic properties. With P. praepinguis as material, lumbrokinase was separated with the salting out method. Lumbrokinase activity was measured with casein medium plate method. Effect of pH and temperature on lumbrokinase activity was studied. Results of lumbrokinase separated from P. praepinguis was relatively high. Lumbrokinase activity in neutral or slightly alkaline environment was higher. Lumbrokinase had tolerance ability to high temperature, with highly enzymatic activity under 60°C and wide range of temperature adaptation. 

THROMBIN PROPERTIES

1957 ◽  
Vol 35 (1) ◽  
pp. 743-758 ◽  
Author(s):  
Edward Ronwin
Keyword(s):  
Ionic Strength ◽  
Substrate Specificity ◽  
Enzymatic Activity ◽  
Enzymatic Properties ◽  
Organic Reagents

The enzymatic properties of thrombin have been examined and compared with those of two related enzymes, plasmin and trypsin. The effects of factors such as pH, substrate specificity, ionic strength, cations, anions, and organic reagents on the enzymatic activity of thrombin have been studied. While the three enzymes discussed possess differences, such similarities as were observed are quite striking and permit their classification into one group as tryptic enzymes.

Molecular activity of sodium pumps in endotherms and ectotherms

1996 ◽  
Vol 271 (5) ◽  
pp. R1287-R1294 ◽  
Author(s):  
P. L. Else ◽  
D. J. Windmill ◽  
V. Markus
Keyword(s):  
Skeletal Muscle ◽  
Enzymatic Activity ◽  
Direct Measurement ◽  
Sodium Pump ◽  
Turnover Rates ◽  
Ouabain Binding ◽  
General Increase ◽  
Sodium Pumps ◽  
Invertebrate Species ◽  
Pump Activity

Previous research has shown ectotherms to have markedly lower sodium pump metabolism than endotherms. Direct measurement of enzymatic activity of the sodium pump (Na(+)-K(+)-adenosinetriphosphatase) confirmed this difference. To determine the source of this difference, sodium pump density was measured with the use of [3H]ouabain binding. Ectotherms and endotherms were found to share similar sodium pump numbers. Approximate densities (in pmol/g) were 250 for skeletal muscle, 500 for liver, 900 for heart, and 8,000 for kidney and brain. Therefore, differences in sodium pump activity between endotherms and ectotherms were due to differences in turnover rates or molecular activities of sodium pumps. Molecular activities of sodium pumps (in ATP/min) of tissues from endotherms were between 6,000 and 12,000 and, for ectotherms, between 1,500 and 2,500. Exceptions were found that included the heart of Bufo marinus. In a single invertebrate species studied, Charax destructor, the sodium pumps of the heart had a low molecular activity characteristic of ectothermic tissues. These results suggest that during the evolution of endothermy there was a general increase in the molecular activity of the sodium pump.

A Conserved Tyrosine Residue of EcSpeG is Absolutely Critical for Enzymatic Activity

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Ee Qi Lim ◽  
Van Le ◽  
Joseph Dang ◽  
Melissa Law ◽  
Misty L. Kuhn
Keyword(s):  
Enzymatic Activity ◽  
Tyrosine Residue ◽  
Conserved Tyrosine

scholarly journals A Novel Aromatic Carboxylic Acid Inhibits Luciferase Enzymatic Activity in Mammalian Cells by Acylation of an Active Regulatory Lysine Residue

2014 ◽  
Vol 106 (2) ◽  
pp. 264a
Author(s):  
Madoka Nakagomi ◽  
Koichi Shudo ◽  
Satoshi Sakamoto ◽  
Hiroshi Handa ◽  
Takeo Iwamoto ◽  
...  
Keyword(s):  
Carboxylic Acid ◽  
Enzymatic Activity ◽  
Mammalian Cells ◽  
Lysine Residue ◽  
Aromatic Carboxylic Acid

scholarly journals Identification of Residues That Affect Oligomerization and/or Enzymatic Activity of Influenza Virus H5N1 Neuraminidase Proteins

2016 ◽  
Vol 90 (20) ◽  
pp. 9457-9470 ◽  
Author(s):  
Meiling Dai ◽  
Hongbo Guo ◽  
Jos C. F. M. Dortmans ◽  
Jojanneke Dekkers ◽  
Johan Nordholm ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Influenza A ◽  
Specific Activity ◽  
Culture Media ◽  
Coiled Coil ◽  
Enzymatic Properties ◽  
Full Length ◽  
Host Tropism ◽  
Head Domain ◽  
Stalk Domain

ABSTRACTInfluenza A virus (IAV) attachment to and release from sialoside receptors is determined by the balance between hemagglutinin (HA) and neuraminidase (NA). The molecular determinants that mediate the specificity and activity of NA are still poorly understood. In this study, we aimed to design the optimal recombinant soluble NA protein to identify residues that affect NA enzymatic activity. To this end, recombinant soluble versions of four different NA proteins from H5N1 viruses were compared with their full-length counterparts. The soluble NA ectodomains were fused to three commonly used tetramerization domains. Our results indicate that the particular oligomerization domain used does not affect theKmvalue but may affect the specific enzymatic activity. This particularly holds true when the stalk domain is included and for NA ectodomains that display a low intrinsic ability to oligomerize. NA ectodomains extended with a Tetrabrachion domain, which forms a nearly parallel four-helix bundle, better mimicked the enzymatic properties of full-length proteins than when other coiled-coil tetramerization domains were used, which probably distort the stalk domain. Comparison of different NA proteins and mutagenic analysis of recombinant soluble versions thereof resulted in the identification of several residues that affected oligomerization of the NA head domain (position 95) and therefore the specific activity or sialic acid binding affinity (Kmvalue; positions 252 and 347). This study demonstrates the potential of using recombinant soluble NA proteins to reveal determinants of NA assembly and enzymatic activity.IMPORTANCEThe IAV HA and NA glycoproteins are important determinants of host tropism and pathogenicity. However, NA is relatively understudied compared to HA. Analysis of soluble versions of these glycoproteins is an attractive way to study their activities, as they are easily purified from cell culture media and applied in downstream assays. In the present study, we analyzed the enzymatic activity of different NA ectodomains with three commonly used tetramerization domains and compared them with full-length NA proteins. By performing a mutagenic analysis, we identified several residues that affected NA assembly, activity, and/or substrate binding. In addition, our results indicate that the design of the recombinant soluble NA protein, including the particular tetramerization domain, is an important determinant for maintaining the enzymatic properties within the head domain. NA ectodomains extended with a Tetrabrachion domain better mimicked the full-length proteins than when the other tetramerization domains were used.

THROMBIN PROPERTIES

1957 ◽  
Vol 35 (9) ◽  
pp. 743-758 ◽  
Author(s):  
Edward Ronwin
Keyword(s):  
Ionic Strength ◽  
Substrate Specificity ◽  
Enzymatic Activity ◽  
Enzymatic Properties ◽  
Organic Reagents

The enzymatic properties of thrombin have been examined and compared with those of two related enzymes, plasmin and trypsin. The effects of factors such as pH, substrate specificity, ionic strength, cations, anions, and organic reagents on the enzymatic activity of thrombin have been studied. While the three enzymes discussed possess differences, such similarities as were observed are quite striking and permit their classification into one group as tryptic enzymes.

scholarly journals Optimization of drying process of Zea Mays malt to use as alternative source of amylolytics enzymes

2005 ◽  
Vol 48 (spe) ◽  
pp. 185-190 ◽  
Author(s):  
Joana Paula Menezes Biazus ◽  
Anderson Gomes Souza ◽  
José Carlos Curvelo Santana ◽  
Roberto Rodrigues de Souza ◽  
Elias Basile Tambougi
Keyword(s):  
Zea Mays ◽  
Enzymatic Activity ◽  
Process Optimization ◽  
Enzymatic Properties ◽  
Process Time ◽  
Drying Process ◽  
Alternative Source

This work aimed to study the drying process optimization of maize (Zea Mays) malt for obtaining maize malt, without affecting enzymatic activity of alpha e beta-amylases from maize malt. Results showed that dryer operation must occur in zone at 54°C and 5.18-6 h process time. The maize malt obtained had good enzymatic properties.

Localization of adenylation site on glutamine synthetase of E. coli by immunoelectron microscopy and image averaging

1984 ◽  
Vol 42 ◽  
pp. 642-643
Author(s):  
T. Wagenknecht ◽  
G. Bronstein ◽  
J. Frank ◽  
R. Frink ◽  
D. Eisenberg ◽  
...  
Keyword(s):  
Glutamine Synthetase ◽  
Enzymatic Activity ◽  
Immunoelectron Microscopy ◽  
Electron Micrographs ◽  
Single Particle ◽  
Tyrosine Residue ◽  
E Coli ◽  
Averaging Methods ◽  
Correlation Methods ◽  
Image Averaging

The glutamine synthetase (GS) from E. coli is a donut-shaped molecule comprising 12 identical subunits arranged in two opposing hexameric layers (dihedral D6 symmetry). In one mode of regulating enzymatic activity, each of the subunits is subject to adenylation at a specific tyrosine residue. A previous study used the technique of immunoelectron microscopy to map the position of adenylation on the surface of the molecule. We describe here a refinement of the analysis be means of computerized single particle averaging methods.Electron micrographs were digitized with a .78 nm sampling distance and images of GS in the six-fold orientation were selected and brought into mutual alignment by correlation methods. The images were divided into two classes depending on whether or not an antibody was visible at the periphery of the molecule. Selected examples of control and antibody-labeled molecules are shown in Fig. la,b respectively.

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