Analyze Diet

The Biochemical journal.

Periodical
Biochemistry
Publisher:
Published by Portland Press on behalf of the Biochemical Society
Frequency: Twenty eight no. a year
Country: England
Language: English
Author(s):
Biochemical Society (Great Britain), Johnston Laboratories. Bio-chemical Department.
Start Year:1906 -
ISSN:
0264-6021 (Print)
1470-8728 (Electronic)
0264-6021 (Linking)
Impact Factor
4.1
2022
NLM ID:257679
(OCoLC):01532962
(DNLM):B14860000(s)
Coden:BIJOAK
LCCN:26011128
Classification:W1 BI621J
The purification of cholinesterase from horse serum.
The Biochemical journal    December 1, 1974   Volume 143, Issue 3 733-744 doi: 10.1042/bj1430733
Main AR, Soucie WG, Buxton IL, Arinc E.A relatively simple method is described by which cholinesterase was purified about 19000-fold starting from horse serum. Typically 20 litres of serum were processed to yield 15-18mg of electrophoretically pure cholinesterase in the form of an active salt-free dry powder. The method included two stages: fractionation with (NH(4))(2)SO(4) and ion-exchange chromatography. The (NH(4))(2)SO(4) stage included, in principle, the acid (pH3) step of the Strelitz (1944) procedure. The step took advantage of the stabilizing effect that 33%-satd. (NH(4))(2)SO(4) has on cholinesterase activity at pH3 and i...
A steady-state kinetic model of butyrylcholinesterase from horse plasma.
The Biochemical journal    September 1, 1974   Volume 141, Issue 3 825-834 doi: 10.1042/bj1410825
Augustinsson KB, Bartfai T, Mannervik B.The steady-state kinetics of the butyrylcholinesterase-catalysed hydrolysis of butyrylthiocholine and thiophenyl acetate were shown to deviate from Michaelis-Menten kinetics. The ;best' empirical rate law was selected by fitting different rate equations to the experimental data by non-linear regression methods. The results were analysed in view of two alternative interpretations: (1) the reaction is catalysed by a mixture of enzymes, or (2) the activity is due to a single enzyme displaying deviations from Michaelis-Menten kinetics. It was concluded that the second alternative applies, and this...
Fractionation of iodinated particles and mitochondria from thyroid by zonal centrifugation and a study of their heterogeneity.
The Biochemical journal    February 1, 1974   Volume 138, Issue 2 299-304 doi: 10.1042/bj1380299
Miquelis R, Simon C.1. The subcellular particles of horse and rat thyroids were fractionated in a B XIV zonal rotor on a non-linear gradient of Ficoll after labelling with radioactive iodine in vitro (horse) or in vivo (rat). In the horse, the resulting fractions were analysed for radioactive iodine, protein and enzymes representative of certain subcellular particles. In the rat, iodine turnover and thyrotrophin stimulation were studied. 2. The population of iodinated particles could be subdivided into three main classes, characterized by differences in beta-galactosidase and acid phosphatase content and position...
The release of iron from horse spleen ferritin to 1,10-phenanthroline.
The Biochemical journal    January 1, 1974   Volume 137, Issue 1 67-70 doi: 10.1042/bj1370067
Hoy TG, Harrison PM, Shabbir M, Macara IG.The rate of release of iron to 1,10-phenanthroline from ferritin fractions of different iron contents has been studied. The experimental results could be interpreted by a simple hypothetical model of the shape of the hydrous ferric oxide micelle at different iron contents, and reasonable correlation obtained between the rate of release and the calculated micelle surface areas. Initial rates of release did not correlate significantly with protein concentration.
The organ-specificity of ferritin in human and horse liver and spleen.
The Biochemical journal    January 1, 1973   Volume 131, Issue 1 51-59 doi: 10.1042/bj1310051
Crichton RR, Millar JA, Cumming RL, Bryce CF.1. Ferritin was isolated from human and horse spleen and liver, and apoferritin prepared therefrom. 2. The electrophoretic mobilities of the four apoferritins were determined on polyacrylamide gels and on cellulose acetate strips, and all found to be equal. 3. Homologous ferritins share reactions of identity in immunodiffusion experiments, whereas heterologous ferritins show only partial identity. 4. The subunit molecular weight of each of the apoferritins was determined by polyacrylamide-gel electrophoresis in sodium dodecyl sulphate and by chromatography on agarose columns in 6m-guanidine-HC...
The binding of carbon dioxide by horse haemoglobin.
The Biochemical journal    August 1, 1971   Volume 124, Issue 1 31-45 doi: 10.1042/bj1240031
Kilmartin JV, Rossi-Bernardi L.1. Three modified horse haemoglobins have been prepared: (i) alpha(c) (2)beta(c) (2), in which both the alpha-amino groups of the alpha- and beta-chains have reacted with cyanate, (ii) alpha(c) (2)beta(2), in which the alpha-amino groups of the alpha-chains have reacted with cyanate, and (iii) alpha(2)beta(c) (2), in which the two alpha-amino groups of the beta-chain have reacted with cyanate. 2. The values of n (the Hill constant) for alpha(c) (2)beta(c) (2), alpha(2)beta(c) (2) and alpha(c) (2)beta(2) were (respectively) 2.5, 2.0 and 2.6, indicating the presence of co-operative interactions ...
Acid-soluble phosphorus compounds in mammalian semen.
The Biochemical journal    August 1, 1970   Volume 118, Issue 5 851-857 doi: 10.1042/bj1180851
Brooks DE.1. A method is described for the extraction, purification and separation of acid-soluble phosphorus compounds from mammalian semen. [8-(14)C]ATP and [8-(14)C]AMP were used as internal recovery standards to measure the breakdown and loss of these nucleotides in the procedure. 2. Bull, ram, boar and stallion semen was separated into seminal plasma and spermatozoa and the two fractions were examined separately. The overall composition of the mixture of the phosphorus compounds extracted from the two fractions was similar for the four species. 3. Glycerylphosphorylcholine and glycerylphosphorylino...
Studies on equine trypsinogen and trypsin.
The Biochemical journal    October 1, 1969   Volume 114, Issue 4 82P doi: 10.1042/bj1140082pa
Harris CI, Hofmann T.No abstract available
The transport of oxidized glutathione from the erythrocytes of various species in the presence of chromate.
The Biochemical journal    October 1, 1969   Volume 114, Issue 4 833-837 doi: 10.1042/bj1140833
Srivastava SK, Beutler E.1. Erythrocytes from normal and glucose 6-phosphate dehydrogenase-deficient humans were subjected to hydrogen peroxide diffusion to oxidize the GSH. Studies were carried out in the presence and absence of chromate to inhibit glutathione reductase and with or without the addition of glucose. 2. The GSH content of erythrocytes from other species was oxidized by subjecting them to hydrogen peroxide diffusion in the presence of chromate and glucose. 3. Chromate (1.3mm) inhibited glutathione reductase by about 80%, whereas glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, hexokin...
Electron-microscopic and chemical studies of oligomers in horse ferritin.
The Biochemical journal    November 1, 1968   Volume 110, Issue 2 265-280 doi: 10.1042/bj1100265
Williams MA, Harrison PM.Horse ferritin was fractionated both by starch-gel electrophoresis and by gel filtration on Sephadex G-200. Monomer fractions contained up to 98% of monomer and oligomer fractions up to 76% of oligomers as determined by quantitative electron microscopy. Percentages obtained from electron micrographs correlated well with analytical starch-gel electrophoretograms and ultracentrifuge patterns. Amino acid analyses of monomer- and oligomer-enriched fractions showed no significant differences. Ferritin oligomers did not apparently dissociate on dilution for electron microscopy or on storage. Apoferr...
Amino acid sequences around the cystine residues in horse growth hormone.
The Biochemical journal    August 1, 1968   Volume 109, Issue 1 19-24 doi: 10.1042/bj1090019
Oliver L, Hartree AS.The cystine-containing peptides of horse growth hormone were isolated and their amino acid sequences determined. Four unique half-cystine residues occur in two peptides, one containing 11 and the other, at the C-terminus of the protein, 15 amino acids. These sequences are compared with published data on growth hormones from other species.
Comparison of the structure of the immunoglobulins from horse serum.
The Biochemical journal    July 1, 1966   Volume 100, Issue 1 63-68 doi: 10.1042/bj1000063
Weir RC, Porter RR.A study of the chemical structure of the horse immunoglobulins IgG and IgA(T) has shown that the amino acid contents of the peptide chains are very similar. These globulins differ most markedly in the products of papain digestion. IgG gives 3.5s products, whereas IgA(T) gives a 5s fraction and smaller components. This difference appears to be associated with the presence of an additional easily reducible disulphide bond in the Fd fragment of the heavy chain. There is two to three times as much carbohydrate in IgA(T) as in IgG. In both, this is in the heavy chain and in IgA(T) more than half is...
Comparative studies on the soluble protein fractions of bovine, equine, porcine and ovine adrenal chromaffin granules.
The Biochemical journal    July 1, 1966   Volume 100, Issue 1 6C-7C doi: 10.1042/bj1000006c
Helle KB.No abstract available.
The action of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin.
The Biochemical journal    September 1, 1965   Volume 96, Issue 3 693-699 doi: 10.1042/bj0960693
Black JA, Leaf G.1. The effects of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin have been investigated. Cytochrome c yielded four fragments, of which two were haemopeptides. The two colourless peptides had amino acid compositions corresponding to those that are expected, on the basis of the sequence proposed for horse-heart cytochrome c by Margoliash, Smith, Kreil & Tuppy (1961), from cleavage at both methionine residues. Of the two haemopeptides, one was isolated and shown to be that derived from cleavage at only one methionine residue, that nearer to the C-terminus of the peptid...
Studies on the binding of 65Zn by equine erythrocytes in vitro.
The Biochemical journal    March 1, 1960   Volume 74, Issue 3 561-567 doi: 10.1042/bj0740561
SIVARAMA SASTRY K, VISWANATHAN L, RAMAIAH A, SARMA PS.No abstract available
Steroids of pregnant mare’s urine. V. Identification of two androstane-3:16-diols; the structure of uranolone.
The Biochemical journal    April 1, 1957   Volume 65, Issue 4 663-668 doi: 10.1042/bj0650663
BROOKS RV, KLYNE W.No abstract available
Potentiometric and other studies on preparations of cytochrome c from ox- and horse-heart muscle.
The Biochemical journal    January 1, 1956   Volume 62, Issue 1 21-29 doi: 10.1042/bj0620021
HENDERSON RW, RAWLINSON WA.No abstract available
The distribution of diphtheria antitoxin in pepsin-digested horse antiserum.
The Biochemical journal    January 1, 1955   Volume 59, Issue 1 47-52 doi: 10.1042/bj0590047
ANDERSON CG.No abstract available
Studies on the composition of horse oil. II. The component fatty acids of lipids from fatty tissues, muscle and liver.
The Biochemical journal    November 1, 1952   Volume 52, Issue 3 400-407 doi: 10.1042/bj0520400
SHORLAND FB, BRUCE LW, JESSOP AS.No abstract available
Steroids of pregnant mares’ urine. IV. Fractionation of the neutral steroids. Examination of some non-ketonic fractions.
The Biochemical journal    August 1, 1952   Volume 51, Issue 5 694-707 doi: 10.1042/bj0510694
BROOKS RV, KLYNE W, MILLER E, PATERSON JY.No abstract available
Some steroids of pregnant mares’ urine; separation by chromatography of benzoates.
The Biochemical journal    August 1, 1951   Volume 49, Issue 3 xl-xli 
BROOKS RV, KLYNE W, MILLER E.No abstract available
The action of acid phosphate on the anion permeability of horse erythrocytes.
The Biochemical journal    June 1, 1951   Volume 49, Issue 1 xix 
HOLTON FA.In 1941, Keilin & Mann described an optical method of studying the penetration of erythrocytes by bicarbonate ions and the intracellular activity of carbonic anhydrase. This method consists of converting the haemoglobin inside the cell to methaemoglobin and observing the transformation of the methaemoglobin from the acid to the alkaline form by the entering bicarbonate ions. During this work they noticed that this transformation did not occur if the methaemoglobin cells had been washed in acid phosphate and interpreted this as an effect on the permeability of the cells. Similar observations by...
The component acids and glycerides of a horse mesenteric fat.
The Biochemical journal    February 1, 1951   Volume 48, Issue 2 137-146 doi: 10.1042/bj0480137
GUPTA SS, HILDITCH TP.No abstract available
The esterases of horse blood; the specificity of horse plasma cholinesterase and ali-esterase.
The Biochemical journal    November 1, 1950   Volume 47, Issue 5 518-525 doi: 10.1042/bj0470518
STURGE LM, WHITTAKER VP.The research article delves into the exploration of the specificity of esterases in horse blood, particularly plasma cholinesterase and the ali-esterase, drawing a clear distinction between the two, which had […]
The esterases of horse blood; the specificity of horse erythrocyte cholinesterase.
The Biochemical journal    November 1, 1950   Volume 47, Issue 5 525-530 doi: 10.1042/bj0470525
MOUNTER LA, WHITTAKER VP.No abstract available
The haemolytic acid present in horse brain; purification and identification as cis-octadec-11-enoic acid.
The Biochemical journal    September 1, 1950   Volume 47, Issue 3 327-330 doi: 10.1042/bj0470327
MORTON ID, TODD AR.No abstract available
The steroids of pregnant mares’ urine; a method for the extraction of steroid sulphates and the isolation of allopregn-16-en-3(beta)-ol-20-one sulphate.
The Biochemical journal    January 1, 1948   Volume 43, Issue 2 231-234 
KLYNE W, SCHACHTER B, MARTIN GF.No abstract available
Vitamin A in the horse.
The Biochemical journal    July 1, 1946   Volume 40, Issue 4 500 
RUDRA MN.No abstract available
A further sulphuric acid ester from the urine of pregnant mares.
The Biochemical journal    January 1, 1946   Volume 40, Issue 5-6 lv 
KLYNE W.No abstract available
The recognition of material present in horse muscle affecting the formation of alpha-toxin by a strain of Clostridium welchii.
The Biochemical journal    January 1, 1946   Volume 40, Issue 3 400-406 doi: 10.1042/bj0400400
Rogers HJ, Knight BC.No abstract available