THE ROLE OF ADSORPTION IN CONTROLLING THE RATE OF REACTION OF CHLORAMBUCIL WITH PROTEIN

1963 ◽  
Vol 41 (1) ◽  
pp. 931-939
Author(s):  
J. H. Linford
Keyword(s):  
Molecular Weight ◽  
Carboxylic Acid ◽  
Bovine Serum Albumin ◽  
Inverse Relationship ◽  
Reaction Rate ◽  
The Other ◽  
Alkylation Reaction ◽  
Rate Of Reaction

Two proteins, haemoglobin and bovine serum albumin, have been studied with respect to their rates of alkylation by chlorambucil in vitro at 37 °C and pH 8.4. The proteins are of nearly the same molecular weight and free carboxylic acid content, but the alkylation reaction is 30 times faster with haemoglobin. On the other hand, the adsorption of chlorambucil by albumin is 20 times greater than that exhibited by haemoglobin. This inverse relationship between extent of adsorption and reaction rate suggests that adsorption protects the chlorambucil from activation in the solvent.

THE ROLE OF ADSORPTION IN CONTROLLING THE RATE OF REACTION OF CHLORAMBUCIL WITH PROTEIN

1963 ◽  
Vol 41 (4) ◽  
pp. 931-939 ◽  
Author(s):  
J. H. Linford
Keyword(s):  
Molecular Weight ◽  
Carboxylic Acid ◽  
Bovine Serum Albumin ◽  
Inverse Relationship ◽  
Reaction Rate ◽  
The Other ◽  
Alkylation Reaction ◽  
Rate Of Reaction

Two proteins, haemoglobin and bovine serum albumin, have been studied with respect to their rates of alkylation by chlorambucil in vitro at 37 °C and pH 8.4. The proteins are of nearly the same molecular weight and free carboxylic acid content, but the alkylation reaction is 30 times faster with haemoglobin. On the other hand, the adsorption of chlorambucil by albumin is 20 times greater than that exhibited by haemoglobin. This inverse relationship between extent of adsorption and reaction rate suggests that adsorption protects the chlorambucil from activation in the solvent.

The role of small molecular weight compounds to increase vacuolation induced by VacA toxin in vitro

2010 ◽  
Vol 24 (5) ◽  
pp. 1373-1378 ◽  
Author(s):  
Juan Sun ◽  
Yan Wu ◽  
Zhuang Su ◽  
Zhifang Liu ◽  
Bingzhong Su ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Small Molecular Weight

In Vitro Characterization Of Low Molecular Weight Fractions Of Heparin

1981 ◽  
Author(s):  
Jawed Fareed ◽  
Harry L Messmore ◽  
Daniel A Walz ◽  
Jean Choay ◽  
J C Lormeau
Keyword(s):  
Molecular Weight ◽  
The Other ◽  
Low Molecular Weight ◽  
In Vitro Test ◽  
Thrombin Time ◽  
Specific Test ◽  
Platelet Factor ◽  
At Iii ◽  
Heparin Fractions

Numerous extraction, chromatographic (ion exchange, gel, and affinity), chemical and enzymatic degradation methods have been employed to obtain heparin fractions. The present assays to evaluate potency (e.g. pharmacopeial and coagulant) do not truly reflect the antithrombotic properties of these fractions. In addition, the synthetic peptide substrate based assays to measure the anti Xa activity do not correlate with the coagulant anti Xa assays. We have developed an in vitro test battery to evaluate low molecular weight heparin fractions. Porcine mucosal heparin fractions are assayed for anti Xa activity in coagulant and amidolytic assays and the results are expressed as a ratio. The effect of these fractions on coagulant assays such as prothrombin time (PT), partial thromboplastin time (PTT), thrombin time (TT), Stypven time (ST) on freshly prepared normal human plasma (NHP) is determined The retention characteristics of these fractions on platelet factor 4 and AT-III bound sepharose columns were also determined. We have compared the extracted and chemically depolymerized heparin fractions and found that the anti Xa activity doesn’t always correlate with the other parameters studied. The extracted fractions were slightly stronger in the USP assays and showed a biphasic retention on the PF-4 column whereas the chemically depolymerized product showed only one peak. On the other hand, on the AT-III column both fractions showed similar elution patterns. Our studies suggest that heparin and its fractions exhibit differential behavior on various assays and a specific test may not be used as an index of the potency of their antithrombotic effects. Furthermore, the potency of these fractions should be stated on a weight basis when evaluated in the in vivo animal models rather than in terms of a specific test (e.g. anti Xa activity and US Pharmacopeial assays).

Imidazole catalyzed silica synthesis: Progress toward understanding the role of histidine in (bio)silicification

2009 ◽  
Vol 24 (5) ◽  
pp. 1700-1708 ◽  
Author(s):  
Mei-Keat Liang ◽  
Siddharth V. Patwardhan ◽  
Elena N. Danilovtseva ◽  
Vadim V. Annenkov ◽  
Carole C. Perry
Keyword(s):  
Molecular Weight ◽  
Silicic Acid ◽  
Catalytic Mechanism ◽  
Synthetic Polymers ◽  
Precipitation Process ◽  
Silica Precipitation ◽  
Silica Synthesis ◽  
Different Molecular Weight

Histidine is an amino acid present in proteins involved in biosilica formation and often found in peptides identified during phage display studies but its role(s) and the extent of its involvement in the silica precipitation process is not fully understood. In this contribution we describe results from an in vitro silicification study conducted using poly-histidine (P-His) and a series of different molecular weight synthetic polymers containing the imidazole functionality (polyvinylimidazole, PVI) for comparison. We show that the presence of imidazole from PVI or P-His is able to catalyze silicic acid condensation; the effect being greater for P-His. The catalytic mechanism is proposed to involve the dual features of the imidazole group—its ability to form hydrogen bonds with silicic acid and electrostatic attraction toward oligomeric silicic acid species.

scholarly journals Delaying meiotic resumption during transportation of bovine cumulus–oocyte complexes: effects on development, apoptosis and caspases activity of in vitro-produced embryos

Zygote ◽  
2017 ◽  
Vol 25 (6) ◽  
pp. 740-750 ◽  
Author(s):  
Priscila Chediek Dall'Acqua ◽  
Beatriz Caetano da Silva Leão ◽  
Nathália Alves de Souza Rocha-Frigoni ◽  
Fernanda Patrícia Gottardi ◽  
Gisele Zoccal Mingoti
Keyword(s):  
Bovine Serum Albumin ◽  
Fetal Calf Serum ◽  
Calf Serum ◽  
The Other ◽  
Developmental Competence ◽  
Bovine Oocyte ◽  
Control Groups ◽  
Meiotic Inhibitors

SummaryThis study examined the effects of meiosis inhibition during bovine oocyte transportation on developmental competence and quality of produced embryos. The transportation medium was supplemented with: 100 μM butyrolactone I (BL), 500 μM IBMX + 100 μM forskolin (mSPOM), 100 μM milrinone (MR) or follicular fluid (bFF), and was carried out in a portable incubator for 6 h. Next, oocytes were in vitro matured (IVM) for 18 h, without the meiotic inhibitors, with the exception of mSPOM group, in which was added 20 μM cilostamide. The three control groups were IVM with 10% fetal calf serum (FCS) (Control Lab FCS) or 0.6% bovine serum albumin (BSA) (Control Lab BSA) in a CO2 in air incubator or in the portable incubator with 0.6% BSA (Control Transp BSA). Higher cleavage rates (P < 0.05) were obtained in the Control Lab FCS group (84.5 ± 5.3%) compared with the other groups (59.6 ± 3.4% to 70.9 ± 2.3%). Embryonic development was higher (P < 0.05) in the Control Lab FCS group (39.8 ± 4.7%) than in the Control Transp BSA (22.7 ± 3.4%) and MR (21.6 ± 2.3%) groups. However, they were similar (P > 0.05) to the other groups (23.6 ± 3.3% to 28.8 ± 2.7%). The total number of blastomeres was higher (P < 0.05) in the Control Lab FCS group (85.2 ± 5.6) than in Control Lab BSA (53.6 ± 2.9), Control Transp BSA (55.5 ± 4.4), BL (58.2 ± 3.0), mSPOM (57.9 ± 4.9) and MR (59.2 ± 3.9), but all these treatments did not differ (P > 0.05) from bFF (67.7 ± 4.2). No differences (P > 0.05) were found in apoptosis by the activity of caspases (139.0 ± 3.2 to 152.4 ± 6.5, expressed in fluorescence intensity) as well as the percentage of TUNEL-positive cells (12.3 ± 2.0% to 15.7 ± 1.7%). In conclusion, the transportation of oocytes over 6 h with BL, mSPOM or bFF enabled the acquisition of developmental competence at similar rates to the Control Lab FCS group.

Prostaglandins and renin release in vitro

1981 ◽  
Vol 240 (6) ◽  
pp. E609-E614
Author(s):  
C. S. Lin ◽  
H. Iwao ◽  
S. Puttkammer ◽  
A. M. Michelakis
Keyword(s):  
Arachidonic Acid ◽  
Renal Cortex ◽  
The Other ◽  
Renin Release ◽  
Eicosatetraenoic Acid ◽  
Juxtaglomerular Cells ◽  
Prostaglandin F2 Alpha ◽  
Prostaglandin System

The present studies were undertaken to explore further the role of prostaglandins in the release of renin from the renal cortex. To provide the best assessment of renin release, renin was determined by a radioimmunoassay for the direct measurement of renin. Slices of mouse renal cortex were incubated at 37 degrees C with arachidonic acid (AA), 5,8,11,14-eicosatetraenoic acid (ETA), indomethacin, prostaglandins, and synthetic prostaglandin endoperoxide analogue (EPA). Our results showed that AA at 1.5 X 10(-8) M significantly increased renin release at 10 and 30 min of incubation. This renin increase ws abolished by either ETA or indomethacin. Prostaglandin F2 alpha (PGF2 alpha) also significantly stimulated renin release at 10 and 60 min. PGE2 and 16,16-dimethyl PGE2 (DMPGE2) showed much less renin release-stimulating activity. EPA and PGI2 on the other hand very strongly stimulated renin release. However, at higher concentrations the stimulating effect of PGI2 and EPA disappeared and even became inhibitory in the case of EPA. Other prostaglandins were found to have no effect on renin release. The results suggest that the prostaglandin system directly affects renin release from the juxtaglomerular cells independent of systemic neurogenic and hemodynamic influences.

Anionic and cationic exchange mechanisms in the skin of anurans, with special reference to Leptodactylidae in vivo

1971 ◽  
Vol 262 (842) ◽  
pp. 163-174 ◽  
Keyword(s):  
Transport Mechanism ◽  
Selective Inhibition ◽  
The Other ◽  
Sodium Absorption ◽  
Experimental Conditions ◽  
Net Flux ◽  
Cationic Exchange

In several species of anurans, the in vivo skin has been shown to absorb Na + and Cl - independently from dilute external solutions. That the mechanism for sodium absorption is different from that of chloride absroption is born out by the following: (1) Either of these ions is absorbed without an accompanying ion when this latter is impermeant. (2) From NaCl solutions there can be an unequal absorption of sodium and chloride. (3) A selective inhibition of the absorption of one of the ions can be produced experimentally, while the net flux of the other remains unchanged. In all these situations, the absorbed ion has to be exchanged against an endogenous ion of the same charge. In Calyptocephalella gayi , H + and HCO - 3 are exchanged against sodium and chloride respectively. A comparison of the relationships between H + excretion and Na + absorption in vivo skins and shortcircuited in vitro skins shows that in the latter no H + excretion occurs, only the Na + transport being maintained under these experimental conditions. From this, one must conclude that the active Na + transport is the motive factor of the transport mechanism. H + excretion by the in vivo skin plays the role of physiologically short-circuiting the Na + transport.

scholarly journals Glucomannan-Mediated Attachment of Rhizobium leguminosarum to Pea Root Hairs Is Required for Competitive Nodule Infection

2008 ◽  
Vol 190 (13) ◽  
pp. 4706-4715 ◽  
Author(s):  
Alan Williams ◽  
Adam Wilkinson ◽  
Martin Krehenbrink ◽  
Daniela M. Russo ◽  
Angeles Zorreguieta ◽  
...  
Keyword(s):  
Biofilm Formation ◽  
Rhizobium Leguminosarum ◽  
Root Hairs ◽  
The Other ◽  
Plant Interactions ◽  
Wild Type ◽  
Polysaccharide Synthesis ◽  
Surface Polysaccharides

ABSTRACT The Rhizobium leguminosarum biovar viciae genome contains several genes predicted to determine surface polysaccharides. Mutants predicted to affect the initial steps of polysaccharide synthesis were identified and characterized. In addition to the known cellulose (cel) and acidic exopolysaccharide (EPS) (pss) genes, we mutated three other loci; one of these loci (gmsA) determines glucomannan synthesis and one (gelA) determines a gel-forming polysaccharide, but the role of the other locus (an exoY-like gene) was not identified. Mutants were tested for attachment and biofilm formation in vitro and on root hairs; the mutant lacking the EPS was defective for both of these characteristics, but mutation of gelA or the exoY-like gene had no effect on either type of attachment. The cellulose (celA) mutant attached and formed normal biofilms in vitro, but it did not form a biofilm on root hairs, although attachment did occur. The cellulose-dependent biofilm on root hairs appears not to be critical for nodulation, because the celA mutant competed with the wild-type for nodule infection. The glucomannan (gmsA) mutant attached and formed normal biofilms in vitro, but it was defective for attachment and biofilm formation on root hairs. Although this mutant formed nodules on peas, it was very strongly outcompeted by the wild type in mixed inoculations, showing that glucomannan is critical for competitive nodulation. The polysaccharide synthesis genes around gmsA are highly conserved among other rhizobia and agrobacteria but are absent from closely related bacteria (such as Brucella spp.) that are not normally plant associated, suggesting that these genes may play a wide role in bacterium-plant interactions.

THE ROLE OF WATER IN THE FORMATION OF SODIUM TRIPHOSPHATE BY CALCINATION

1954 ◽  
Vol 32 (12) ◽  
pp. 1100-1111 ◽  
Author(s):  
J. D. McGilvery ◽  
A. E. Scott
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Reaction Rate ◽  
Ionic Diffusion ◽  
Fusion Point ◽  
Rapid Formation

The formation of sodium triphosphate by calcination, below the sodium triphosphate fusion point, of various phosphate mixtures of over-all composition 5Na2O.3P2O5.xH2O was investigated. Water plays an important role, decreasing the amounts of pyrophosphate and high molecular weight polyphosphate impurities and increasing the reaction rate under certain conditions. It is suggested that water catalyzes the reactions by: (1) facilitating ionic diffusion, (2) hydrolyzing —P—O—P—linkages, and (3) assisting in the crystallization of sodium triphosphate. With ortho- and pyro-phosphate mixtures temperatures of about 300 °C. and higher are necessary for the rapid formation of sodium triphosphate. With glasses of the composition 5Na2O.3P2O5 good yields may be obtained at temperatures as low as 250 °C. when water is present.

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