scholarly journals GLUTARALDEHYDE FIXATION OF ISOLATED EUCARYOTIC NUCLEI

1973 ◽  
Vol 59 (2) ◽  
pp. 304-317 ◽  
Author(s):  
Donald E. Olins ◽  
Everline B. Wright
Keyword(s):  
Free Amino ◽  
Divalent Cations ◽  
Amino Groups ◽  
Chromatin Decondensation ◽  
Mole Percent ◽  
First Order ◽  
Close Proximity ◽  
Erythrocyte Nucleus ◽  
Fixation Reaction ◽  
Kinetics Of

Isolated chicken erythrocyte nuclei have been incubated with dilute concentrations of the bifunctional cross-linking agent glutaraldehyde (0–20 mM) in order to stabilize histone-histone interactions within the native nucleus. The kinetics of the disappearance of acid-soluble histones, free amino groups, and of individual histones have been observed to be pseudo first-order. Apparent first-order rate constants for the disappearance of individual histones correlate with the lysine mole percent of that fraction and follow the ranking, kapp: F1 > F2C > F2B ≥ F2A2, F2A1, F3. Histone polymers were observed to form very rapidly during the fixation reaction. Partial fractionation and amino acid analyses of these polymers support the view that they are composed principally of cross-linked (F2C)n molecules (where n = 2 to ∼8). The rate of glutaraldehyde reaction with free amino groups in histones is drastically reduced in solvents that promote chromatin decondensation (i.e., low ionic strengths in the absence of divalent cations) whereas the formation of cross-linked F2C polymers is less severely reduced. It is proposed that some F2C histones exist in close proximity within the isolated erythrocyte nucleus.

scholarly journals Amino-functionalized (meth)acryl polymers by use of a solvent-polarity sensitive protecting group (Br-t-BOC)

2016 ◽  
Vol 12 ◽  
pp. 245-252
Author(s):  
Helmut Ritter ◽  
Monir Tabatabai ◽  
Markus Herrmann
Keyword(s):  
Free Radical ◽  
Nmr Spectroscopy ◽  
Free Amino ◽  
Solvent Polarity ◽  
Protecting Group ◽  
Amino Groups ◽  
Neighboring Group ◽  
H Nmr ◽  
Polarity Sensitive ◽  
Kinetics Of

We describe the synthesis of bromo-tert-butyloxycarbonyl (Br-t-BOC)-amino-protected monomers 2-((1-bromo-2-methylpropan-2-yl)oxycarbonylamino)ethyl (meth)acrylate 3a,b. For this purpose, 2-isocyanatoethyl (meth)acrylate 1a,b was reacted with 1-bromo-2-methylpropan-2-ol (2a). The free radical polymerization of (Br-t-BOC)-aminoethyl (meth)acrylates 3a,b yielded poly((Br-t-BOC)-aminoethyl (meth)acrylate) 6a,b bearing protected amino side groups. The subsequent solvolysis of the Br-t-BOC function led to the new polymers poly(2-aminoethyl (meth)acrylate) 8a,b with protonated free amino groups. The monomers and the resulting polymers were thoroughly characterized by 1H NMR, IR, GPC and DSC methods. The kinetics of the deprotection step was followed by 1H NMR spectroscopy. The solvent polarity and neighboring group effects on the kinetics of deprotection are discussed.

Epimerization of lactose to free lactulose in heated model milk solutions

1985 ◽  
Vol 52 (3) ◽  
pp. 409-417 ◽  
Author(s):  
Barry D. Greig ◽  
Gerald A. Payne
Keyword(s):  
Thermal Effects ◽  
Amino Sugar ◽  
The Other ◽  
Processing Conditions ◽  
Amino Groups ◽  
First Order ◽  
Base Catalysts ◽  
The Difference ◽  
Kinetics Of

SUMMARYThe kinetics of the epimerization of lactose to lactulose were determined for two ‘model milk’ solutions, one containing lactose and the other lactose and lysine. The lysine was added to lactose to determine whether amino groups of proteins act as base catalysts promoting the production of free lactulose. The presence of lysine actually reduced the rate of production of free lactulose, presumably by the formation of amino-sugar complexes. The rate of production of free lactulose over the range of processing conditions was shown to be first order for both systems. Thermal effects on lactose were shown to be complex. The epimerization of lactose to lactulose was reversible and both sugars were thermally decomposed to their monosaccharides. The difference in the rate of production of free lactulose between the lactose, and the lactose and lysine solutions was also observed in processed milk and its ultrafiltrate (protein free).

scholarly journals THE STABILITY OF BACTERIAL VIRUSES IN SOLUTIONS OF SALTS

1949 ◽  
Vol 32 (5) ◽  
pp. 579-594 ◽  
Author(s):  
Mark H. Adams
Keyword(s):  
Metal Ion ◽  
Divalent Cations ◽  
Order Reaction ◽  
Sodium Salts ◽  
E Coli ◽  
First Order ◽  
Bacterial Viruses ◽  
Effects Of Temperature ◽  
The Stability ◽  
Kinetics Of

1. The seven bacterial viruses of the T group, active against E. coli, are much more rapidly inactivated by heat when suspended in 0.1 N solutions of sodium salts than when suspended in broth. 2. The kinetics of this inactivation whether in salt solutions or in broth are those of a first order reaction. 3. The rate of inactivation of phage T5 in 0.1 N NaCl at 37°C. can be greatly decreased by the addition of 10–8 M concentrations of such divalent cations as Ca, Mg, Ba, Sr, Mn, Co, Ni, Zn, Cd, and Cu. 4. An increase in the cation concentration in the suspending medium results in an increase in the stability of phage T5 to the inactivating effects of temperature. 5. The hypothesis is proposed that the increase in stability of phage T5 in the presence of various cations is the result of complex formation between the phage and the metal ion.

Kinetische und proteinchemische Untersuchungen am Succinyl-Papain / Kinetic and Chemical Investigations of Succinyl-Papain

1972 ◽  
Vol 27 (12) ◽  
pp. 1490-1497 ◽  
Author(s):  
H. G. Löffler ◽  
Fr. Schneider
Keyword(s):  
Free Amino ◽  
Succinic Anhydride ◽  
Kinetic Studies ◽  
Amino Groups ◽  
Native State ◽  
Limited Effect ◽  
X Ray ◽  
The Stability ◽  
Kinetics Of ◽  
Increased Activity

Kinetic studies of the reaction of papain with succinic anhydride demonstrate the reactivity of 10 amino groups, two of which are easily deacylated giving a stable succinylpapain with 3 free amino groups one of which is the free amino group of the terminal isoleucin. This modified enzyme has the tenfold solubility of papain between pH 5,9 - 9 and is a little more sensible to temperature than papain. Kinetic parameters of succinylpapain with N-Benzoyl-ʟ-arginine ethylester are: Km app =1,2 x 10-2 ᴍ( papain: 1,8 x 10-2 M) κcat=505 min-1 (papain: 475 min-1) at pH 6,2 and 37°C. The activity with the anionic substrate casein was 120 ± 10%, with the cationic protamine was 200 ± 20% of the activity of papain.Nitration of 17 ± 1 tyrosines of succinylpapain with tetranitromethane has only a limited effect on the activity of the enzyme. The kinetics of this reaction suggests the existence of three groups of tyrosines with different reactivity. The reaction of papain with tetranitromethane gives only insoluble, cross-linked products.Three of five present tryptophanes of papain and succinylpapain are oxidized by N-bromosuccinimide in the native state; in 8 ᴍ urea all residues are accessible. The esterase- and proteolytic activity of the oxidized enzyme decrease to less than 50% of controls while with benzoyl-ᴅ, ʟ-arginine-p-nitro-anilide there was observed an increased activity of about 250%. The stability of the enzyme drops considerably after oxidation of five tryptophane residues. Function and reactivity of the modified amino acids are discussed with regard to the results of the x-ray analysis of the enzyme

scholarly journals The reaction of 2,4,6-trinitrobenzenesulphonic acid with amino acids, peptides and proteins

1968 ◽  
Vol 108 (3) ◽  
pp. 383-391 ◽  
Author(s):  
R. B. Freedman ◽  
G. K. Radda
Keyword(s):  
Amino Acids ◽  
Glutamate Dehydrogenase ◽  
Free Amino ◽  
Reactive Species ◽  
Second Order ◽  
Amino Group ◽  
Exponential Rate ◽  
Amino Groups ◽  
Sh Group ◽  
Kinetics Of

1. The kinetics of the reaction of 2,4,6-trinitrobenzenesulphonic acid with various amino acids, peptides and proteins were studied by spectrophotometry. 2. The reaction of the α- and ∈-amino groups in simple amino acids was found to be second-order, and the unprotonated amino group was shown to be the reactive species. 3. By allowing for the concentration of unreactive −NH3+ group, intrinsic reactivities for the free amino groups were derived and shown to be correlated with the basicities. 4. The SH group of N-acetylcysteine was found to be more reactive to 2,4,6-trinitrobenzenesulphonic acid than most amino groups. 5. The reactions of insulin, chymotrypsinogen and ribonuclease with 2,4,6-trinitrobenzenesulphonic acid were analysed in terms of three exponential rate curves, each referring to one or more amino groups of the proteins. 6. The reaction of lysozyme with 2,4,6-trinitrobenzenesulphonic acid was found to display an acceleration effect. 7. From the reaction of 2,4,6-trinitrobenzenesulphonic acid with glutamate dehydrogenase at several enzyme concentrations, it was possible to discern two sets of amino groups of different reactivity, and to show that the number of groups in each set was decreased by aggregation of the enzyme.

COMPARATIVE STUDIES OF THE POTENTIATION OF CORTICOTROPHIN ACTIVITY BY SEVERAL INACTIVE DERIVATIVES

1963 ◽  
Vol 42 (2) ◽  
pp. 209-213 ◽  
Author(s):  
Arthur I. Cohen ◽  
Edward H. Frieden
Keyword(s):  
Biological Activity ◽  
Comparative Studies ◽  
Free Amino ◽  
Hormonal Activity ◽  
Amino Groups

ABSTRACT A number of corticotrophin analogues have been prepared, some of which potentiate the biological activity of the untreated hormone in vitro. The free amino groups of corticotrophin appear to be essential not only for hormonal activity, but also for the interaction of the analogues with the tissue corticotrophin inactivating system which is assumed to account for the potentiating effect.

Kinetic of oxidation of methyl orange by vanadium(V) under conditions VO2+ and decavanadates coexist: Catalysis by Triton X-100 micellar medium

2019 ◽  
Author(s):  
Chem Int
Keyword(s):  
Methyl Orange ◽  
Solution Ph ◽  
Vanadium Concentration ◽  
Limiting Behavior ◽  
First Order ◽  
First Order Kinetics ◽  
Ph Range ◽  
Kinetic Pattern ◽  
Triton X ◽  
Kinetics Of

The kinetics of oxidation of methyl orange by vanadium(V) {V(V)} has been investigated in the pH range 2.3-3.79. In this pH range V(V) exists both in the form of decavanadates and VO2+. The kinetic results are distinctly different from the results obtained for the same reaction in highly acidic solution (pH < 1) where V(V) exists only in the form of VO2+. The reaction obeys first order kinetics with respect to methyl orange but the rate has very little dependence on total vanadium concentration. The reaction is accelerated by H+ ion but the dependence of rate on [H+] is less than that corresponding to first order dependence. The equilibrium between decavanadates and VO2+ explains the different kinetic pattern observed in this pH range. The reaction is markedly accelerated by Triton X-100 micelles. The rate-[surfactant] profile shows a limiting behavior indicative of a unimolecular pathway in the micellar pseudophase.

The Kinetics of Glucose Decomposition with Sulfate Reduction in the Anaerobic Fluidized Bed Reactor

1993 ◽  
Vol 28 (2) ◽  
pp. 135-144 ◽  
Author(s):  
S. Matsui ◽  
R. Ikemoto Yamamoto ◽  
Y. Tsuchiya ◽  
B. Inanc
Keyword(s):  
Sulfate Reduction ◽  
Fluidized Bed ◽  
Kinetic Equations ◽  
Fluidized Bed Reactor ◽  
Order Reaction ◽  
First Order Reaction ◽  
First Order ◽  
Glucose Decomposition ◽  
Reaction Equations ◽  
Kinetics Of

Using a fluidized bed reactor, experiments on glucose decomposition with and without sulfate reduction were conducted. Glucose in the reactor was mainly decomposed into lactate and ethanol. Lactate was mainly decomposed into propionate and acetate, while ethanol was decomposed into propionate, acetate, and hydrogen. Sulfate reduction was not involved in the decomposition of glucose, lactate, and ethanol, but was related to propionate and acetate decomposition. The stepwise reactions were modeled using either a Monod expression or first order reaction kinetics in respect to the reactions. The coefficients of the kinetic equations were determined experimentally. The modified Monod and first order reaction equations were effective at predicting concentrations of glucose, lactate, ethanol, propionate, acetate, and sulfate along the beight of the reactor. With sulfate reduction, propionate was decomposed into acetate, while without sulfate reduction, accumulation of propionate was observed in the reactor. Sulfate reduction accelerated propionate conversion into acetate by decreasing the hydrogen concentration.

Submerged upflow biotower operation and computer simulation

1994 ◽  
Vol 30 (11) ◽  
pp. 143-146
Author(s):  
Ronald D. Neufeld ◽  
Christopher A. Badali ◽  
Dennis Powers ◽  
Christopher Carson
Keyword(s):  
Computer Simulation ◽  
Benzoic Acid ◽  
Computer Model ◽  
Rate Constants ◽  
Batch Mode ◽  
Operational Conditions ◽  
First Order ◽  
Low Concentrations ◽  
Biological Transformation ◽  
Kinetics Of

A two step operation is proposed for the biodegradation of low concentrations (< 10 mg/L) of BETX substances in an up flow submerged biotower configuration. Step 1 involves growth of a lush biofilm using benzoic acid in a batch mode. Step 2 involves a longer term biological transformation of BETX. Kinetics of biotransformations are modeled using first order assumptions, with rate constants being a function of benzoic acid dosages used in Step 1. A calibrated computer model is developed and presented to predict the degree of transformation and biomass level throughout the tower under a variety of inlet and design operational conditions.

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