scholarly journals THE STAGES OF THE PEPTIC HYDROLYSIS OF EGG ALBUMIN

1927 ◽  
Vol 10 (3) ◽  
pp. 437-450 ◽  
Author(s):  
Jennie McFarlane ◽  
Violet E. Dunbar ◽  
Henry Borsook ◽  
Hardolph Wasteneys
Keyword(s):  
Protein Molecule ◽  
Total N ◽  
Egg Albumin ◽  
Hydrolysis Of

1. Most of the products of the peptic hydrolysis of albumin, about 85 per cent of the total N, are primary in the sense that they arise directly from the protein molecule, and undergo no further hydrolysis. 2. A slow secondary hydrolysis, involving about 15 per cent of the total N, occurs in the proteose and simpler fractions primarily split off. 3. Acid metaprotein in peptic hydrolysis arises as a result of the action of acid. It is not an essential stage in the hydrolysis of undenatured albumin. 4. Acid metaprotein is hydrolyzed by pepsin more slowly under comparable conditions than undenatured albumin.

Determination of Unconjugated and Total N-Acetyl-p-aminophenol (NAPA) in Urine and Serum

1967 ◽  
Vol 13 (3) ◽  
pp. 215-219 ◽  
Author(s):  
Karel P M Heirwegh ◽  
Johan Fevery
Keyword(s):  
Liver Disease ◽  
Acid Hydrolysis ◽  
Azo Dye ◽  
Acidic Medium ◽  
Diazonium Salt ◽  
Accurate Method ◽  
Total N ◽  
Hydrolysis Of ◽  
Urine And Serum

Abstract A sensitive and accurate method is described for the determination of N-acetyl-p-aminophenol (NAPA) and its metabolites in urine and serum. In strongly acidic medium, p-aminophenol (PAP) resulting from differential extraction and acid hydrolysis of total NAPA and unconjugated NAPA, is diazotized and the diazonium salt coupled with N-(1-naphthyl)ethylenediamine (NED) in the presence of ethanol. The blue azo dye formed is determined spectrophotometrically. Application to liver disease is briefly reported.

A simple procedure using trinitrobenzenesulphonic acid for monitoring proteolysis in cheese

1988 ◽  
Vol 55 (4) ◽  
pp. 585-596 ◽  
Author(s):  
Anna Polychroniadou
Keyword(s):  
Simple Procedure ◽  
Water Soluble ◽  
Acid Solutions ◽  
Amino Groups ◽  
Total N ◽  
Cheese Ripening ◽  
Amino Acid Solutions ◽  
Hydrolysis Of ◽  
Good Agreement

SummaryA simple, rapid and sensitive spectrophotometric assay was developed and evaluated for monitoring proteolysis during cheese ripening, based on the fact that α-amino groups released by hydrolysis of cheese proteins react with trinitrobenzenesulphonic acid to form products that absorb strongly at 420 nm. A linear relationship was shown to exist between A420 and concentration of free α amino groups up to 0·5 HIM (r = 0·999, 38 df, P < 0·001). Repeatability of the method was satisfactory. The coefficient of variance was 0·53% for amino acid solutions and 1·19% for cheese extracts. Average recovery of glycine added to the cheese was 104 ± 2·9%. A comparison of the above method with that of determination of water-soluble N to total N ratio showed that there was good agreement between these two methods of assessment of proteolysis in cheese (r = 0·857, 32 df, P < 0·001). Mainly Feta and Teleme cheese were examined, but a similar correlation was obtained with hard Greek cheeses. Analytical conditions of the procedure are discussed.

Study and modeling of mechanisms of cholinesterasis reactions in order to improve their catalytic properties in the neutralization reactions of organophosphorous compounds

2020 ◽  
pp. 134-174
Author(s):  
Sergey Varfolomeev ◽  
Bella Grigorenko ◽  
Sofya Lushchekina ◽  
Patrick Masson ◽  
Galina Mahaeva ◽  
...  
Keyword(s):  
First Generation ◽  
Organophosphorus Compounds ◽  
Protein Molecule ◽  
Catalytic Antibodies ◽  
High Rate ◽  
Biological Targets ◽  
Organophosphorous Compounds ◽  
Rate Of Hydrolysis ◽  
The Stability ◽  
Hydrolysis Of

“Biocleaners” or “bioscavengers” are biological objects (enzymes, catalytic antibodies) that are capable of binding and/or hydrolyzing organophosphorus compounds (OPC). Their use seems to be the most effective alternative to traditional antidotes to neutralize or detoxify OPC. The introduction of bioscavengers allows neutralizing toxicant molecules in the bloodstream before they reach their biological targets, thereby providing protection against poisoning. Bioscavengers of the first-generation neutralized OPC molecules by stoichiometrically binding to them. The safety and efficacy of human butyrylcholinesterase (BChE) for protecting against OPC poisoning has been shown. However, the stoichiometric neutralization of OPC requires the introduction of a huge amount of expensive biopharmaceuticals. Catalytic bioscavengers that hydrolytically neutralize OPC were introduced at a much lower dose to achieve the same degree of effectiveness. The most effective catalytic bioscavengers are enzymes. The most promising enzymes are artificial mammalian paraoxonase mutants and bacterial phosphotriesterases. However, studies of other enzymes, such as prolidases, oxidases, artificial mutants of cholinesterases and carboxyl esterases and catalytic antibodies are actively ongoing. Since OPC are pseudosubstrates of cholinesterases (ChEs), a detailed description of the mechanisms of inhibition, dealkylation, and spontaneous reactivation of phosphorylated ChEs is critical for the development of ChEs mutants with a high rate of hydrolysis of OPC. The review presents an analysis of different views on the mechanisms of interaction of ChEs with OPC, discusses the possible directions of creating effective catalytic biological traps based on BChE and changes in their mechanism of action as compared to the native enzyme. A separate section is devoted to the effect of mutations, both polymorphic and artificial, on the stability of the protein molecule of BChE.

SOME FACTORS INFLUENCING THE BINDING OF L-THYROXINE BY PROTEINS

1961 ◽  
Vol 36 (2) ◽  
pp. 230-236 ◽  
Author(s):  
L. Korsgaard Christensen
Keyword(s):  
Structural Changes ◽  
Considerable Increase ◽  
Serum Proteins ◽  
Binding Capacity ◽  
Protein Molecule ◽  
Binding Property ◽  
Moderate Increase ◽  
Urea Denaturation ◽  
Egg Albumin ◽  
Releasing Effect

ABSTRACT The pH-dependence of the binding of L-thyroxine to the serum proteins has been investigated by means of a dialysis procedure. A moderate increase in the binding of T4 was found when the pH varied from about 7 to 8.5. At more alkaline and more acid values a pronounced decrease in the ability to bind thyroxine was observed. The use of barbiturate buffer resulted in a very considerable increase in free non-protein-bound T4, whereas phosphate buffer did not interfere with the binding of the hormone. Tris buffer has also a thyroxine-releasing effect but this is far less pronounced than for barbiturate. Structural changes in the protein molecule were found to change its ability to bind T4. Urea denaturation of bovine serum albumin resulted in a decreased binding capacity, whereas denatured egg albumin and lactoglobulin exhibited an increase in binding property.

THE PROTEOLYTIC ENZYMES OF MICROORGANISMS: III. SOME CHARACTERISTICS OF EXTRACELLULAR PROTEASES PRODUCED IN SUBMERGED CULTURE

1950 ◽  
Vol 28c (6) ◽  
pp. 600-612 ◽  
Author(s):  
W. B. McConnell
Keyword(s):  
Low Temperatures ◽  
Free Amino ◽  
Submerged Culture ◽  
Culture Medium ◽  
Proteolytic Enzymes ◽  
Amino Groups ◽  
Extracellular Proteases ◽  
Egg Albumin ◽  
Rapid Hydrolysis ◽  
Hydrolysis Of

Some of the general characteristics of the proteases liberated into the culture medium by molds and actinomycetes grown in submerged culture have been studied. Species of Alternaria, Streptomyces, Mortierella, and Gliocladium were used. The enzymes resemble trypsin in that they are most active at a pH slightly above 7 and are inhibited by a preparation of egg albumin. They are stable at low temperatures but suffer marked losses in activity when stored for 16 hr. above 40 °C. The most rapid hydrolysis of gelatin occurs at temperatures between 40 °C. and 50 °C. The enzymes from different organisms show definite differences with respect to their ability to attack different proteins, gelatin and casein being in general the most readily digested. The protease systems from different organisms also vary with respect to the extent to which they can digest gelatin; some enzymes are able to release about three times as many amino groups from gelatin as others. The limit of the hydrolysis is not dependent upon substrate concentration but is slightly affected by the concentration of enzyme. The enzymes were effective in liberating free amino acids from gelatin.

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 QUANTITATIVE EXPERIMENTS WITH ANTIBODIES TO A SPECIFIC PRECIPITATE. I

1941 ◽  
Vol 73 (1) ◽  
pp. 125-140 ◽  
Author(s):  
Henry P. Treffers ◽  
Michael Heidelberger
Keyword(s):  
Horse Serum ◽  
Serum Antibody ◽  
Protein Molecule ◽  
Antigenic Specificity ◽  
Rabbit Serum ◽  
Type I ◽  
Egg Albumin ◽  
Homologous Antigen ◽  
Antibody Function ◽  
Immune Rabbit

1. Rabbits were injected with the washed specific precipitate from Type II antipneumococcus horse serum. Antibody in the resulting antiserum was determined by the quantitative agglutinin method using various specific precipitates as antigens. 2. Suspensions of Types I and II antipneumococcus horse specific precipitates, as well as the specific precipitates derived from Type VIII Pn (anti-C portion), and H. influenzae horse antisera were found to remove the same amount of antibody from the immune rabbit serum. 3. Purified antibody solutions prepared by dissociation methods from Types I and II antipneumococcus horse sera were found to remove the same quantity of antibody as did the homologous specific precipitates. 4. Specific precipitates from anti-crystalline egg albumin and anti-diphtheria horse sera were found to remove only a fraction of the antibody. The reasons for this are discussed. 5. A specific precipitate prepared from pepsin-digested Type I anti-pneumococcus horse serum removed all of the antibody to the homologous antigen from the rabbit anti-precipitate serum, but followed a different quantitative course. 6. From the quantitative course of these reactions and from experiments with specific precipitates from anti-Pn rabbit and pig sera it is concluded that the only antigenic specificity demonstrable for the antibodies investigated was that due to their common origin, and that the groupings responsible for their antibody function constitute either a small part of the total protein molecule or else are non-antigenic.

scholarly journals On the existence of an unidentified sulphur grouping in the protein molecule. Part I.—On the denaturation of proteins

1923 ◽  
Vol 94 (663) ◽  
pp. 426-441 ◽  
Keyword(s):  
Amino Acid ◽  
Protein Molecule ◽  
Egg White ◽  
Dissociation Product ◽  
Decomposition Products ◽  
Actual Form ◽  
Protein Substance ◽  
Points Of View ◽  
Hydrolysis Of ◽  
Denaturation Of Proteins

The hydrolysis of a protein substance which contains sulphur almost invariably results in the production of cystine among the decomposition products. This amino-acid almost certainly represents the actual form in which the bulk of the sulphur is combined in the molecule of most proteins. Cystine is, indeed, the only sulphur-body so far isolated which can be regarded with certainty as a primary dissociation product of protein. At the same time, there is a certain amount of evidence to suggest that in certain proteins—notably ovalbumin, and also casein—some of the sulphur is present in a form other than cystine. In the research about to be described this question was investigated mainly from two points of view:— (1) An examination was made of certain reactions given by egg white (and its products), attributable to sulphur groupings other than cystine. In the course of this work some light was thrown on the chemistry of denaturation.

STANDARD ISOTOPE VERSUS NITROGEN BALANCE CRITERIA FOR ASSESSING THE EFFICIENCY OF NITROGEN SOURCES FOR BARLEY

1973 ◽  
Vol 53 (1) ◽  
pp. 73-77 ◽  
Author(s):  
R. J. RENNIE ◽  
D. A. RENNIE
Keyword(s):  
Nitrogen Balance ◽  
Nitrogen Sources ◽  
Fertilizer N ◽  
N Application ◽  
Total N ◽  
Plant System ◽  
Plant Parts ◽  
Solonetzic Soil ◽  
Causative Factors ◽  
Hydrolysis Of

Nitrogen balance (fertilizer N accounted for in the soil–plant system) and standard isotope (obtained on above-ground plant parts) criteria were used to evaluate the efficiency of nitrogen sources for barley grown on a Chernozemic and a Solonetzic soil under greenhouse conditions. The isotope criteria, percent total N in the plant tissue derived from fertilizer (% N d.f.f.), "A" values, and uptake of fertilizer N by the crop, clearly indicated the superiority, in terms of plant availability, of the NO3−-N source, followed by NH4+-N, with urea the least effective. In contrast, loss of nitrogen from the soil–plant system was greatest for the NO3−-N and least for the urea (i.e., 67 vs. 26% on the Solonetzic soil). Such conflicting results can be explained on the basis of slow hydrolysis of the urea and rapid plant uptake of N from the NO3−-N form. It is concluded that, although isotope-derived criteria such as % N d.f.f., A values, and uptake by the crop of fertilizer N provide precise measurements of the performance of N sources, serious errors in causative factors may be made unless "nitrogen balance" data are available. The significance of primary and corrected (rate of fertilizer N application corrected for fertilizer N loss) A values are discussed.

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