Inhibition of lactate dehydrogenase ex rabbit muscle by Cibacron Blue 3G-A bound to water-soluble hydroxyethylcellulose

1985 ◽  
Vol 50 (6) ◽  
pp. 1335-1340 ◽  
Author(s):  
Danica Mislovičová ◽  
Peter Gemeiner ◽  
Ladislav Šoltés
Keyword(s):  
Lactate Dehydrogenase ◽  
Molecular Mass ◽  
Covalent Binding ◽  
Polymeric Matrix ◽  
Water Soluble ◽  
Rabbit Muscle ◽  
Cibacron Blue ◽  
Molecular Masses

The interaction between lactate dehydrogenase and hydroxyethylcellulose - Cibacron Blue 3G-A conjugates was investigated kinetically. These conjugates were obtained by covalent binding of Cibacron Blue to water-soluble hydroxyethylcelluloses, of average relative molecular masses 2.5 . 104 to 11.6 . 104. The polymeric matrix (non-branched β-glucan) was, unlike the branched α-glucans, found to inhibit the action of the dye, irrespective of the molecular mass of this matrix. With increasing amount of the bound dye the interaction between the dye and the enzyme was enhanced.

Antrachinon-triazine derivatives of polysaccharides, affinity of bovine heart lactate dehydrogenase to Cibacron Blue derivatives of water-soluble dextran fractions and hydroxyethyl-starches

1984 ◽  
Vol 49 (2) ◽  
pp. 549-554 ◽  
Author(s):  
Jana Barthová ◽  
Marie Tichá ◽  
Peter Gemeiner ◽  
Danica Mislovičová
Keyword(s):  
Lactate Dehydrogenase ◽  
Molecular Mass ◽  
Water Soluble ◽  
Relative Molecular Mass ◽  
Cibacron Blue ◽  
Strength Of Interaction ◽  
Triazine Derivatives ◽  
Starch Derivatives ◽  
Derivatives Of ◽  
Hydroxyethyl Starches

The interaction of lactate dehydrogenase with high-molecular-weight derivatives of Cibacron Blue was followed by measuring the reaction kinetics and by means of affinity electrophoresis. The dye was covalently bound to dextrans with relative molecular mass ranging from 5 000 to 2 000 000 and to hydroxyethyl-starches with relative molecular mass from 130 000 to 2 000 000. In the case of dextran derivatives of Cibacron Blue, various degrees of substitution by the dye were tested. Measurement of kinetics showed that the Cibacron Blue derivatives competed with NADH for the binding site on the enzyme and that when the dye was bound to a polysaccharide, the affinity of lactate dehydrogenase to the dye decreased. Both methods used confirmed that the strength of interaction did not depend on the relative molecular mass of the polysaccharide carrier or on the degree of substitution. The interaction of lactate dehydrogenase with hydroxyethyl-starch derivatives of Cibacron Blue was weaker than with dextran derivatives.

Antraquinone-triazine derivatives of polysaccharides. Relation between structure and affinity to lactate dehydrogenase

1981 ◽  
Vol 46 (2) ◽  
pp. 419-427 ◽  
Author(s):  
Peter Gemeiner ◽  
Danica Mislovičová ◽  
Jiří Zemek ◽  
Ľudovít Kuniak
Keyword(s):  
Lactate Dehydrogenase ◽  
Degree Of Substitution ◽  
Brilliant Blue ◽  
Rabbit Muscle ◽  
Muscle Lactate ◽  
Cibacron Blue ◽  
Triazine Derivatives ◽  
Covalently Linked ◽  
The Relationship ◽  
Derivatives Of

The inhibition effects (I50) of a series of dyes (Cibacrom Blue 3G-A, Procion Blue MX-R, Remazo Brilliant Blue and Ostazin Brilliant Red S5-B) covalently linked to dextran T 70 were the criterion of the relationship between the structure of antraquinone-triazine compounds and their affinity to rabbit muscle lactate dehydrogenase (LDH). The I50 values indicate a substantial importance of the terminal benzenesulfonane moiety in the structure of Cibacron Blue. Also the degree of substitution of polysaccharide plays an important role in the affinity; its influence upon I50 can be expressed for Cibacron Blue-Dextrans T 70 by an equation of line. The influence of the structure of the polysaccharide constituent on the affinity of Cibacron Blue-(α-glucans) towards LDH is discussed, as well.

Characterization of dissolved material during the initial phase of softwood kraft pulping

TAPPI Journal ◽  
2013 ◽  
Vol 12 (1) ◽  
pp. 37-43 ◽  
Author(s):  
HANNU PAKKANEN ◽  
TEEMU PALOHEIMO ◽  
RAIMO ALÉN
Keyword(s):  
Mass Transfer ◽  
Molecular Mass ◽  
Initial Phase ◽  
Degradation Products ◽  
Kraft Pulping ◽  
Reaction Products ◽  
Cooking Temperature ◽  
Molecular Masses ◽  
Aliphatic Carboxylic Acids

The influence of various cooking parameters, such as effective alkali, cooking temperature, and cooking time on the formation of high molecular mass lignin-derived and low molecular mass carbohydrates-derived (aliphatic carboxylic acids) degradation products, mainly during the initial phase of softwood kraft pulping was studied. In addition, the mass transfer of all of these degradation products was clarified based on their concentrations in the cooking liquor inside and outside of the chips. The results indicated that the degradation of the major hemicellulose component, galactoglucomannan, typically was dependent on temperature, and the maximum degradation amount was about 60%. In addition, about 60 min at 284°F (140°C) was needed for leveling off the concentrations of the characteristic reaction products (3,4-dideoxy-pentonic and glucoisosaccharinic acids) between these cooking liquors. Compared with low molecular mass aliphatic acids, the mass transfer of soluble lignin fragments with much higher molecular masses was clearly slower.

scholarly journals Nanomechanical Molecular Mass Sensing Using Suspended Microchannel Resonators

Sensors ◽  
2021 ◽  
Vol 21 (10) ◽  
pp. 3337
Author(s):  
Alberto Martín-Pérez ◽  
Daniel Ramos ◽  
Javier Tamayo ◽  
Montserrat Calleja
Keyword(s):  
Molecular Mass ◽  
Mass Density ◽  
Applied Pressure ◽  
Atomic Mass ◽  
Liquid Sample ◽  
Mass Sensing ◽  
Average Molecular Mass ◽  
Fluid Properties ◽  
Molecular Masses ◽  
Microchannel Resonators

In this work we study the different phenomena taking place when a hydrostatic pressure is applied in the inner fluid of a suspended microchannel resonator. Additionally to pressure-induced stiffness terms, we have theoretically predicted and experimentally demonstrated that the pressure also induces mass effects which depend on both the applied pressure and the fluid properties. We have used these phenomena to characterize the frequency response of the device as a function of the fluid compressibility and molecular masses of different fluids ranging from liquids to gases. The proposed device in this work can measure the mass density of an unknown liquid sample with a resolution of 0.7 µg/mL and perform gas mixtures characterization by measuring its average molecular mass with a resolution of 0.01 atomic mass units.

scholarly journals Kinetic Studies of Rabbit Muscle Lactate Dehydrogenase

1962 ◽  
Vol 237 (5) ◽  
pp. 1668-1675
Author(s):  
Virginia Zewe ◽  
Herbert J. Fromm
Keyword(s):  
Lactate Dehydrogenase ◽  
Kinetic Studies ◽  
Rabbit Muscle ◽  
Muscle Lactate

scholarly journals Chiral Selectors in Capillary Electrophoresis: Trends During 2017–2018

Molecules ◽  
2019 ◽  
Vol 24 (6) ◽  
pp. 1135 ◽  
Author(s):  
Raymond B. Yu ◽  
Joselito P. Quirino
Keyword(s):  
Capillary Electrophoresis ◽  
Molecular Mass ◽  
Chiral Separation ◽  
Chiral Separations ◽  
Water Soluble ◽  
Resonance Spectroscopy ◽  
Electrokinetic Chromatography ◽  
Chiral Selectors ◽  
Analytical Technique ◽  
Pharmaceutical Industries

Chiral separation is an important process in the chemical and pharmaceutical industries. From the analytical chemistry perspective, chiral separation is required for assessing the fit-for-purpose and the safety of chemical products. Capillary electrophoresis, in the electrokinetic chromatography mode is an established analytical technique for chiral separations. A water-soluble chiral selector is typically used. This review therefore examines the use of various chiral selectors in electrokinetic chromatography during 2017–2018. The chiral selectors were both low and high (macromolecules) molecular mass molecules as well as molecular aggregates (supramolecules). There were 58 papers found by search in Scopus, indicating continuous and active activity in this research area. The macromolecules were sugar-, amino acid-, and nucleic acid-based polymers. The supramolecules were bile salt micelles. The low molecular mass selectors were mainly ionic liquids and complexes with a central ion. A majority of the papers were on the use or preparation of sugar-based macromolecules, e.g., native or derivatised cyclodextrins. Studies to explain chiral recognition of macromolecular and supramolecular chiral selectors were mainly done by molecular modelling and nuclear magnetic resonance spectroscopy. Demonstrations were predominantly on drug analysis for the separation of racemates.

scholarly journals Identification of two highly sialylated human tear-fluid DMBT1 isoforms: the major high-molecular-mass glycoproteins in human tears

2002 ◽  
Vol 366 (2) ◽  
pp. 511-520 ◽  
Author(s):  
Benjamin L. SCHULZ ◽  
David OXLEY ◽  
Nicolle H. PACKER ◽  
Niclas G. KARLSSON
Keyword(s):  
Molecular Mass ◽  
Peptide Mass Fingerprinting ◽  
High Molecular Mass ◽  
Tear Fluid ◽  
Protein Variant ◽  
Peptide Mass ◽  
Composite Gel ◽  
Molecular Masses ◽  
Protein Components ◽  
Sialyl Lea

Human open eye tear fluid was separated by low-percentage SDS/PAGE to detect high-molecular-mass protein components. Two bands were found with apparent molecular masses of 330 and 270kDa respectively. By peptide-mass fingerprinting after tryptic digestion, the proteins were found to be isoforms of the DMBT1 gene product, with over 30% of the predicted protein covered by the tryptic peptides. By using gradient SDS/agarose/polyacrylamide composite gel electrophoresis and staining for glycosylation, it was shown that the two isoforms were the major high-molecular-mass glycoproteins of >200kDa in human tear fluid. Western blotting showed that the proteins expressed sialyl-Lea. After the release of oligosaccharides by reductive β-elimination from protein blotted on to PVDF membrane, it was revealed by liquid chromatography-MS that the O-linked oligosaccharides were comprised mainly of highly sialylated oligosaccharides with up to 16 monosaccharide units. A majority of the oligosaccharides could be described by the formula dHex0→2NeuAc1→xHexxHexNAcx(-ol), x = 1–6, where Hex stands for hexose, dHex for deoxyhexose, HexNAc for N-acetylhexosamine and NeuAc for N-acetylneuraminate. The number of sialic acids in the formula is less than 5. Interpretation of collision-induced fragmentation tandem MS confirmed the presence of sialic acid and suggested the presence of previously undescribed structures carrying the sialyl-Lea epitopes. Small amounts of neutral and sulphated species were also present. This is the first time that O-linked oligosaccharides have been detected and described from protein variant of the DMBT1 gene.

scholarly journals Evaluation of equilibrium constants for the interaction of lactate dehydrogenase isoenzymes with reduced nicotinamide-adenine dinucleotide by affinity chromatography

1975 ◽  
Vol 151 (3) ◽  
pp. 631-636 ◽  
Author(s):  
R I Brinkworth ◽  
C J Masters ◽  
D J Winzor
Keyword(s):  
Lactate Dehydrogenase ◽  
Affinity Chromatography ◽  
Equilibrium Constants ◽  
Mouse Tissue ◽  
Rabbit Muscle ◽  
Muscle Lactate ◽  
Sodium Phosphate Buffer ◽  
A Value ◽  
Series Of Experiments ◽  
Reduced Nicotinamide Adenine Dinucleotide

Rabbit muscle lactate dehydrogenase was subjected to frontal affinity chromatography on Sepharose-oxamate in the presence of various concentrations of NADH and sodium phosphate buffer (0.05 M, pH 6.8) containing 0.5 M-NaCl. Quantitative interpretation of the results yields an intrinsic association constant of 9.0 × 104M−1 for the interaction of enzyme with NADH at 5°C, a value that is confirmed by equilibrium-binding measurements. In a second series of experiments, zonal affinity chromatography of a mouse tissue extract under the same conditions was used to evaluate assoication constants of the order 2 × 105M−1, 3 × 105M−1, 4 × 105M−1, 7 × 105M−1 and 2 × 106M−1 for the interaction of NADH with the M4, M3H, M2H2, MH3 and H4 isoenzymes respectively of lactate dehydrogenase.

Dynamic computed tomography with low- and high-molecular-mass contrast agents to assess microvascular permeability modifications in a model of liver fibrosis

2002 ◽  
Vol 103 (2) ◽  
pp. 213-216 ◽  
Author(s):  
Roland MATERNE ◽  
Laurence ANNET ◽  
Stéphane DECHAMBRE ◽  
Christine SEMPOUX ◽  
Anne M. SMITH ◽  
...  
Keyword(s):  
Liver Fibrosis ◽  
Contrast Agents ◽  
Molecular Mass ◽  
Hepatic Fibrosis ◽  
Mean Transit Time ◽  
Distribution Volume ◽  
High Molecular Mass ◽  
Permeability Changes ◽  
Molecular Masses ◽  
The Mean

Interstitial collagen formation and transformation of the fenestrated hepatic sinusoids into continuous capillaries are major ultrastructural changes that occur in liver cirrhosis and fibrosis. These modifications lead to progressive restriction of blood–liver exchanges. The purpose of our study was to evaluate the permeability changes in a model of hepatic fibrosis by using dynamic computed tomography (CT) enhanced with contrast agents of different molecular masses. Dynamic single-section CT of the liver was performed after intravenous bolus administration of a low-molecular-mass contrast agent (iobitridol) and an experimental high-molecular-mass agent (P840) in normal control rabbits and in rabbits with hepatic fibrosis. Hepatic, aortic and portal venous time–density curves were fitted with a dual-input one-compartmental model to calculate the hepatic mean transit time and distribution volume of the contrast agents. In the rabbits with liver fibrosis, the mean transit time of the high-molecular-mass agent was shorter than that of the low-molecular-mass agent (10.0±1.8s and 12.0±1.2s respectively; P<0.05). The distribution volume accessible to the high-molecular-mass agent was also smaller (22.2±4.8% compared with 32.0±6.7%; P<0.01). In the normal rabbits, the mean transit times of the high- and low-molecular-mass agents did not differ significantly, and nor did their distribution volumes. Our results demonstrate decreased sinusoidal permeability for the high-molecular-mass agent P840 in a model of hepatic fibrosis. Non-invasive assessment of permeability changes in liver fibrosis can be performed with dynamic CT and contrast agents of different molecular masses.

scholarly journals Mass spectrometric analysis of rat liver cytosolic glutathione S-transferases: modifications are limited to N-terminal processing

1995 ◽  
Vol 308 (1) ◽  
pp. 69-75 ◽  
Author(s):  
H I Yeh ◽  
C H Hsieh ◽  
L Y Wang ◽  
S P Tsai ◽  
H Y Hsu ◽  
...  
Keyword(s):  
Molecular Mass ◽  
Female Rats ◽  
Spectrometric Analysis ◽  
Affinity Column ◽  
Female Rat ◽  
Significant Difference ◽  
Cytosolic Glutathione ◽  
Glutathione S Transferases ◽  
Molecular Masses ◽  
Rat Livers

Cytosolic glutathione S-transferases (GSTs) from rat livers were purified using an S-hexylglutathione affinity column. The GST subunits were resolved by reverse-phase HPLC and their molecular masses were determined by electrospray mass spectrometry. The major hepatic GSTs detected were subunits 1, 1′, 2, 3 and 4, with molecular mass of 25,520, 25,473, 25,188, 25,782 and 25,571 Da respectively. Subunits 6, 7 and 10 are minor components, with molecular mass of 25,551, 23,308 and 25,211 Da respectively. Alternatively, the hepatic GSTs were purified using a glutathione affinity column. Subunits 1, 1′, 2, 8 and 10 were eluted from this column with GSSG, the oxidized form of glutathione. Subunit 8 has a molecular mass of 25,553 Da. The remaining proteins on the glutathione affinity column were removed with glutathione and S-hexylglutathione. Subunits 2, 3, 4 and 6 could be detected in the eluate. We could not detect any significant difference in molecular mass between GSTs isolated from male and female rat livers. Cytosolic GSTs were isolated from livers of buthionine sulphoximine-treated female rats for MS analysis. The molecular masses obtained were identical to those determined for the controls.

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