Kinetics of the Inhibition of Plasmin in Acidified Human Plasma

1982 ◽  
Vol 48 (03) ◽  
pp. 257-259 ◽  
Author(s):  
H R Lijnen ◽  
M Maes ◽  
M Castel ◽  
M Samama ◽  
D Collen
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Competitive Inhibitor ◽  
Normal Plasma ◽  
Competitive Inhibitors ◽  
Rate Of Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of

SummaryAcid-treated human plasma is a competitive inhibitor of the hydrolysis of D-Val-Leu-Lys-Nan (S-2251) by plasmin. The rate of hydrolysis is decreased to 50% by 750 fold diluted acidified normal plasma and by 60 fold diluted acidified α2-antiplasmin depleted plasma (α2-antiplasmin concentration less than 2%). These findings suggest that α2-antiplasmin is a contributary but not the main competitive inhibitor of acidified plasma. This interpretation is supported by the finding that α2-antiplasmin depleted plasma reconstituted with purified α2-antiplasmin inhibits the hydrolysis of S-2251 by plasmin at a 125 fold dilution following acidification and by the finding that in a purified system acid inactivated α2-antiplasmin inhibits the hydrolysis of S-2251 by plasmin with a Ki of 25 nM. Thus, besides α2-antiplasmin, other plasma proteins which are at least in part eliminated by the removal of α2-antiplasmin from plasma by immunoadsorption appear to be competitive inhibitors for plasmin in acidified plasma. It is suggested that several competitive inhibitors for plasmin are present and/or generated in acidified plasma and that these inhibitors may at least in part be responsible for the variability in the results of measurements of plasminogen and/or plasmin in plasma following acidification.

Kinetics of hydrolysis of peroxodisulphate ions in acidic medium to peroxomonosulphuric acid

1981 ◽  
Vol 46 (5) ◽  
pp. 1229-1236 ◽  
Author(s):  
Jan Balej ◽  
Milada Thumová
Keyword(s):  
Ionic Strength ◽  
Rate Constants ◽  
Acidic Medium ◽  
Measured Data ◽  
Molar Ratios ◽  
Starting Solution ◽  
Kinetics Of Hydrolysis ◽  
Rate Of Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of

The rate of hydrolysis of S2O82- ions in acidic medium to peroxomonosulphuric acid was measured at 20 and 30 °C. The composition of the starting solution corresponded to the anolyte flowing out from an electrolyser for production of this acid or its ammonium salt at various degrees of conversion and starting molar ratios of sulphuric acid to ammonium sulphate. The measured data served to calculate the rate constants at both temperatures on the basis of the earlier proposed mechanism of the hydrolysis, and their dependence on the ionic strength was studied.

Mechanistic Information from the Effect of Pressure on the Kinetics of Hydrolysis of Iodopentaaquochromium(III) Ion

1975 ◽  
Vol 53 (24) ◽  
pp. 3697-3701 ◽  
Author(s):  
Milton Cornelius Weekes ◽  
Thomas Wilson Swaddle
Keyword(s):  
Ionic Strength ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Hydrogen Ion Concentration ◽  
Kinetics Of Hydrolysis ◽  
Rate Of Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Aqueous Hclo ◽  
Conjugate Base

The rate of hydrolysis of iodopentaaquochromium(III) ion has been measured as a function of pressure (0.1 to 250 MPa) and hydrogen ion concentration (0.1 to 1.0 mol kg−1) at 298.2 K and ionic strength 1.0 mol kg−1 (aqueous HClO4–LiClO4). The volumes of activation for the acid independent and inversely acid dependent hydrolysis pathways are −5.4 ± 0.5 and −1.6 ± 0.3 cm3 mol−1 respectively, and are not detectably pressure-dependent. Consideration of these values, together with the molar volume change of −3.3 ± 0.3 cm3 mol−1 determined dilatometrically for the completed hydrolysis reaction, indicates that the mechanisms of the two pathways are associative interchange (Ia) and dissociative conjugate base (Dcb) respectively.

A Raman Spectral Study of the Kinetics of Hydrolysis of Acetonitrile Catalyzed by Hg(II)

1975 ◽  
Vol 53 (3) ◽  
pp. 427-436 ◽  
Author(s):  
Yu-Keung Sze ◽  
Donald E. Irish
Keyword(s):  
Time Span ◽  
Water Molecules ◽  
Specific Rate ◽  
Ammine Complexes ◽  
Kinetics Of Hydrolysis ◽  
Specific Rate Constant ◽  
Rate Of Hydrolysis ◽  
Raman Spectral ◽  
Kinetics Of ◽  
Hydrolysis Of

Raman spectroscopy has been employed to follow the relatively slow rate of hydrolysis of acetonitrile, catalyzed by mercury(II). Raman lines at 2275 and 2305 cm−1 are characteristic of CH3CN bound to Hg2+, and are distinct from lines of bulk solvent. The intensities of these new lines decrease with time. From the intensities, concentrations of bound acetonitrile, [CH3CN]B were calculated for a time span of 400 min. The data fit a second order rate law: Rate = k[CH3CN]B[H2O]. The specific rate constant, k, obtained from four sets of data for the system Hg(ClO4)2–CH3CN–H2O equals 1.05 ± 0.06 × 10−4 mol−1 1 min−1 at 25 °C. The energy of activation is 18.9 kcal mol−1. In the proposed mechanism water molecules attack acetonitrile molecules which are bound to Hg2+ and form a mercury(II)–acetamide complex. Raman lines characteristic of this species are observed. This species slowly converts to mercury(II) ammine complexes and acetic acid. Anions which coordinate with Hg2+ more strongly than CH3CN, such as nitrate or acetate, slow or prevent the hydrolysis reaction.

Kinetics of hydrolysis of meclofenoxate hydrochloride in human plasma

1987 ◽  
Vol 39 (3) ◽  
pp. 215-218 ◽  
Author(s):  
Sumie Yoshioka ◽  
Yukio Aso ◽  
Mitsuru Uchiyama
Keyword(s):  
Human Plasma ◽  
Kinetics Of Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of

scholarly journals Hydrolysis of Adenosine Triphosphate by Crystalline Yeast Pyrophosphatase

1962 ◽  
Vol 45 (4) ◽  
pp. 31-46 ◽  
Author(s):  
M. Kunitz
Keyword(s):  
Ion Exchange ◽  
Protein Molecule ◽  
Molar Ratio ◽  
Inorganic Pyrophosphatase ◽  
Inorganic Pyrophosphate ◽  
Rate Of Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Zn Ions ◽  
Dowex 1

Schlesinger and Coon's report that crystalline yeast inorganic pyrophosphatase, in addition to its known ability to hydrolyze inorganic pyrophosphate in the presence of Mg ions, is also able to catalyze the hydrolysis of ATP and ADP in the presence of Zn ions was confirmed. A systematic study showed that the ratio of 370 of PPase-Mg over ATPase-Zn activities per milligram protein in various preparations of pyrophosphatase obtained in the course of isolation of crystalline pyrophosphatase from baker's yeast was nearly identical in all the preparations, independent of their purity. The course of hydrolysis of ATP by crystalline pyrophosphatase in the presence of Zn was carried out with the aid of ion exchange on Dowex 1. The finding of Schlesinger and Coon that the hydrolysis proceeds from ATP to ADP and then slowly to AMP was confirmed. The kinetics of the first phase of the reaction was found to depend on the molar ratio of Zn/ATP in the reaction mixture. Mg ions in the presence of Zn ions have an accelerating effect on the rate of hydrolysis of ATP. This suggests strongly that both activities—ATPase and PPase—are manifestations of the same active group in the protein molecule of crystalline pyrophosphatase.

scholarly journals The kinetics of hydrolysis of some extended N-aminoacyl-l-arginine methyl esters by human plasma kallikrein. Evidence for subsites S2 and S3

1982 ◽  
Vol 203 (1) ◽  
pp. 149-153 ◽  
Author(s):  
P R Levison ◽  
G Tomalin
Keyword(s):  
Human Plasma ◽  
Methyl Esters ◽  
Plasma Kallikrein ◽  
Substrate Complex ◽  
Enzyme Substrate ◽  
Rate Limiting Step ◽  
Kinetics Of Hydrolysis ◽  
Rate Limiting ◽  
Kinetics Of ◽  
Hydrolysis Of

Subsites in the S2-S4 region were identified in human plasma kallikrein. Kinetic constants (kcat., Km) were determined for a series of seven extended N-aminoacyl-L-arginine methyl esters based on the C-terminal sequence of bradykinin (-Pro-Phe-Arg) or (Gly)n-Arg. The rate-limiting step for the enzyme-catalysed reaction was found to be deacylation of the enzyme. It was possible to infer that hydrogen-bonded interactions occur between substrate and the S2-S4 region of kallikrein. Insertion of L-phenylalanine at residue P2 demonstrates that there is also a hydrophobic interaction with subsite S2, which stabilizes the enzyme-substrate complex. The strong interaction demonstrated between L-proline at residue P3 and subsite S3 is of greatest importance in the selectivity of human plasma kallikrein. The purification of kallikrein from Cohn fraction IV of human plasma is described making use of endogenous Factor XIIf to activate the prekallikrein. Kallikreins I (Mr 91 000) and II (Mr 85 000) were purified 170- and 110-fold respectively. Kallikrein I was used for the kinetic work.

scholarly journals Phenylcarbamic acid derivatives with integrated n-phenylpiperazine moiety in the structure – kinetics of alkaline hydrolysis study / Deriváty kyseliny fenylkarbámovej s integrovanou n-fenylpiperazínovou zložkou v štruktúre – štúdium kinetiky alkalickej hydrolýzy

2015 ◽  
Vol 62 (2) ◽  
pp. 38-42
Author(s):  
Stankovičová M. ◽  
Miháliková V. ◽  
Mezovský Ľ. ◽  
Lašáková A. ◽  
Medlenová V. ◽  
...  
Keyword(s):  
Alkaline Hydrolysis ◽  
Phenyl Ring ◽  
Arrhenius Equation ◽  
Sodium Hydroxide Solution ◽  
Antimycobacterial Activity ◽  
First Order ◽  
Rate Of Hydrolysis ◽  
Pseudo First Order ◽  
Kinetics Of ◽  
Hydrolysis Of

AbstractIn present work, we have studied kinetics of alkaline hydrolysis of 14 compounds, which are phenylcarbamic acid derivatives with integrated N-phenylpiperazine moiety in the structure. The compounds possessed moderate antiarrhythmic and antimycobacterial activity. Their hydrolysis was carried out in an aqueous medium ethanol sodium hydroxide solution. The course of the hydrolysis was observed spectrophotometrically in visible as well as in ultraviolet regions. The pseudo-first order rate constants were calculated at several temperatures. The values of the activation energy EAwere determined by the Arrhenius equation. The rate of hydrolysis of the compounds under the study increase with the increase in temperature and it has been differentiated according to the substitution of N-phenylpiperazine as well as to the alkoxy substitution on phenyl ring.

scholarly journals The reaction of alkylating agents with bacteriophage R17. Biological effects of phosphotriester formation

1974 ◽  
Vol 137 (2) ◽  
pp. 313-317 ◽  
Author(s):  
Kenneth V. Shooter ◽  
Ruth Howse ◽  
R. Kenneth Merrifield
Keyword(s):  
Reaction Mechanism ◽  
Biological Effects ◽  
Alkylating Agents ◽  
Hydrolysis Reaction ◽  
Ethyl Methanesulphonate ◽  
Neutral Ph ◽  
Rate Of Hydrolysis ◽  
Alkylation Reactions ◽  
Kinetics Of ◽  
Hydrolysis Of

The extent of biological inactivation and of the degradation of the RNA after reaction of bacteriophage R17 with ethyl methanesulphonate, isopropyl methanesulphonate and N-ethyl-N-nitrosourea was studied. Formation of breaks in the RNA chain probably results from hydrolysis of phosphotriesters formed in the alkylation reactions. Near neutral pH the ethyl and isopropyl phosphotriesters are sufficiently stable for the kinetics of the hydrolysis reaction to be followed. Results indicate that the rate of hydrolysis increases rapidly as the pH is raised. The evidence shows that a phosphotriester group does not itself constitute a lethal lesion. The extent of phosphotriester formation by the different agents is discussed in terms of reaction mechanism.

Diagnostic Enzymology of a-L-Iduronidase with Special Reference to a Sulphated Disaccharide Derived from Heparin

1982 ◽  
Vol 62 (2) ◽  
pp. 193-201 ◽  
Author(s):  
J. J. Hopwood ◽  
Vivienne Muller
Keyword(s):  
Enzyme Activity ◽  
Competitive Inhibitor ◽  
Ph Profile ◽  
Ph Values ◽  
Substrate Structure ◽  
Cultured Skin ◽  
Bivalent Cations ◽  
Competitive Inhibitors ◽  
Specific Ion Effect ◽  
Hydrolysis Of

1. Iduronosyl anhydro[1-3H]mannitol 6-sulphate (IMs), iduronosyl anhydro[1-3H]mannitol, phenyl iduronide (PhI) and 4-methylumbelliferyl iduronide have been compared as substrates for the diagnostic estimation of α-l-iduronidase activity present in human leucocyte and cultured skin fibroblast homogenates. The pH profile of leucocyte and fibroblast iduronidase activity was dependent on substrate structure and concentration, the ionic strength and the nature of the buffer ion used in the assay mixture. 2. NaCl, KBr and Na2SO4 were shown to be parabolic competitive inhibitors of IMs activity, the K1 with fibroblast homogenates being 34, 13.4 and 0.22 mmol/l respectively. NaCl and KBr were shown to have a primary salt effect on the interaction between enzyme and substrate but Na2SO4 appeared to have a specific ion effect at a cationic binding site. 3. NaCl inhibited the hydrolysis of IMs at all pH values studied, whereas NaCl concentrations of 0.2 mol/l inhibited the hydrolysis of PhI at pH values below 3.8 but activated the enzyme at higher incubation pH values. 4. Cu2+ was shown to be a potent non-competitive inhibitor of IMs enzyme activity with an apparent Kl, of approximately 0.02 mmol/l. The enzyme activity was inhibited by Fe2+ (Kl 4 mmol/l), Hg2+ and Ag+, but has not significantly been affected by other univalent or bivalent cations. 5. The presence of solvent and salt effects on apparent Km but not the Vmax. suggest that the binding of IMs to the enzyme involved charge neutralization, and it is inferred that two cationic binding sites are present at the active site. It is postulated that one site specifically binds to the iduronic acid carboxyl group, the other to the 6-sulphate of the anhydromannitol moiety.

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