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)
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 isolation of a new sulphuric acid ester from the urine of pregnant mares.
The Biochemical journal
January 1, 1945
Volume 39, Issue 5 xlv
KLYNE W, MARRIAN GF.No abstract available The Blood of Equines.
The Biochemical journal
January 1, 1922
Volume 16, Issue 6 770-779 doi: 10.1042/bj0160770
Neser CP.No abstract available The enzymic reduction and kinetics of oxidation of cytochrome b-245 of neutrophils.
The Biochemical journal
May 15, 1982
Volume 204, Issue 2 479-485 doi: 10.1042/bj2040479
Cross AR, Higson FK, Jones OT, Harper AM, Segal AW.1. The absorption coefficient of human neutrophil plasma-membrane reduced-minus-oxidized cytochrome b-245 was determined [delta epsilon (mM; 559-540 nm) = 21.6 cm-1]. 2. Neutrophil polymorphonuclear leucocytes (neutrophils) were prepared from human, ox, horse and pig blood. In each case plasma-membrane fractions were found to contain low-potential cytochrome b. When membranes from horse neutrophils were incubated anaerobically with either NADH or NADPH the cytochrome b became reduced. Prior stimulation of the cells with phorbol myristate acetate did not increase the rate or extent of cytochrom... Read More
57
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 ... Read More
31
Uterocalin, a lipocalin provisioning the preattachment equine conceptus: fatty acid and retinol binding properties, and structural characterization.
The Biochemical journal
May 23, 2001
Volume 356, Issue Pt 2 369-376 doi: 10.1042/0264-6021:3560369
Suire S, Stewart F, Beauchamp J, Kennedy MW.The equine conceptus is surrounded by a fibrous capsule that persists until about day 20 of pregnancy, whereupon the capsule is lost, the conceptus attaches to the endometrium and placentation proceeds. Before attachment, the endometrium secretes in abundance a protein of the lipocalin family, uterocalin. The cessation of secretion coincides with the end of the period during which the conceptus is enclosed in its capsule, suggesting that uterocalin is essential for the support of the embryo before direct contact between maternal and foetal tissues is established. Using recombinant protein and ... Read More
24
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 […] Read More
19
Isolation and characterization of latherin, a surface-active protein from horse sweat.
The Biochemical journal
May 1, 1986
Volume 235, Issue 3 645-650 doi: 10.1042/bj2350645
Beeley JG, Eason R, Snow DH.A protein, latherin, with unusual surface activity was isolated from horse sweat by gel filtration and ion-exchange chromatography. The protein has a Stokes radius, determined by gel filtration, of 2.47 nm, and in the ultracentrifuge sediments as a single species with S20,W 2.05 S, indicating an Mr of 24,400. On SDS/polyacrylamide-gel electrophoresis the molecule behaves as a single peptide chain of apparent Mr 20,000. Latherin contains a high proportion of hydrophobic amino acids (37.2%), and the leucine content (24.5%) is exceptionally high. The unusual composition of the protein may account... Read More
18
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... Read More
18
Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c.
The Biochemical journal
August 15, 1987
Volume 246, Issue 1 43-54 doi: 10.1042/bj2460043
Gadsby PM, Peterson J, Foote N, Greenwood C, Thomson AJ.Magnetic-circular-dichroism (m.c.d.) spectra over the wavelength range 300-2000 nm at room temperature and at 4.2K of horse heart cytochrome c are reported at a series of pH values between 7.8 and 11.0, encompassing the alkaline transition. The effect of glassing agents on the e.p.r. spectrum at various pH values is also reported. Comparison of these results with spectra obtained for the n-butylamine adduct of soybean leghaemoglobin support the hypothesis that lysine is the sixth ligand in the alkaline form of horse heart cytochrome c. The m.c.d. and e.p.r. spectra of horse heart cytochrome c ... Read More
18
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 Read More
17
Use of procainamide gels in the purification of human and horse serum cholinesterases.
The Biochemical journal
April 1, 1983
Volume 211, Issue 1 243-250 doi: 10.1042/bj2110243
Ralston JS, Main AR, Kilpatrick BF, Chasson AL.Two large-scale methods based primarily on the use of procainamide-Sepharose gels were developed for the purification of horse and human serum non-specific cholinesterases. With method I, the procainamide-Sepharose 4B gel was used in the first step to handle large volumes of serum. With method II, the procainamide-Sepharose 4B gel was used in the final step to obtain pure enzyme. Although both methods gave electrophoretically pure cholinesterase preparations in good yields, they were significantly more efficient at purifying the horse enzyme than the human enzyme. To study this problem, the re... Read More
16
A cytochrome c mutant with high electron transfer and antioxidant activities but devoid of apoptogenic effect.
The Biochemical journal
March 7, 2002
Volume 362, Issue Pt 3 749-754 doi: 10.1042/0264-6021:3620749
Abdullaev ZKh, Bodrova ME, Chernyak BV, Dolgikh DA, Kluck RM, Pereverzev MO, Arseniev AS, Efremov RG, Kirpichnikov MP, Mokhova EN, Newmeyer DD....A cytochrome c mutant lacking apoptogenic function but competent in electron transfer and antioxidant activities has been constructed. To this end, mutant species of horse and yeast cytochromes c with substitutions in the N-terminal alpha-helix or position 72 were obtained. It was found that yeast cytochrome c was much less effective than the horse protein in activating respiration of rat liver mitoplasts deficient in endogenous cytochrome c as well as in inhibition of H(2)O(2) production by the initial segment of the respiratory chain of intact rat heart mitochondria. The major role in the di... Read More
15
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 Read More
14
The pH dependence of naturally occurring low-spin forms of methaemoglobin and metmyoglobin: an EPR study.
The Biochemical journal
October 24, 2000
Volume 351 Pt 3, Issue Pt 3 595-605
Svistunenko DA, Sharpe MA, Nicholls P, Blenkinsop C, Davies NA, Dunne J, Wilson MT, Cooper CE.The paramagnetic species in human metHb and horse metmyoglobin (metMb) have been studied at low temperature using EPR spectroscopy. The high-spin (HS) haem signal in aquometMb has a greater rhombic distortion than the HS metHb signal. Nevertheless, the individual line width (g=6) is smaller in metMb than in metHb, consistent with non-identical signals from the alpha and beta Hb subunits. Three low-spin (LS) haem forms are present in metHb, while metMb has only two. The major LS form in both proteins is the alkaline species (with OH(-) at the sixth co-ordination position). The minor LS forms ar... Read More
13
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... Read More
13
Purification of chicken liver ferritin by two novel methods and structural comparison with horse spleen ferritin.
The Biochemical journal
March 1, 1989
Volume 258, Issue 2 413-419 doi: 10.1042/bj2580413
Passaniti A, Roth TF.Ferritin was purified from chicken liver by two different methods: gel filtration on controlled-pore glass beads, and immunoaffinity chromatography employing a chicken ferritin-specific monoclonal antibody that did not cross-react with horse spleen ferritin. This antibody recognizes intact ferritin and an oligomeric 240 kDa form of the molecule after protein transfer to nitrocellulose, but not the 22 kDa chicken ferritin subunit. Chicken liver ferritin purified by these methods exhibited reduced migration on non-denaturing polyacrylamide gels compared with horse spleen ferritin. These results ... Read More
13
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... Read More
12
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... Read More
12
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 Read More
10
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. Read More
10
A 19 kDa protein secreted by the endometrium of the mare is a novel member of the lipocalin family.
The Biochemical journal
November 15, 1996
Volume 320 ( Pt 1), Issue Pt 1 137-143 doi: 10.1042/bj3200137
Crossett B, Allen WR, Stewart F.Large quantities of an unusual 19 kDa protein (p19) are secreted into the lumen of the uterus of the mare (Equus caballus) during the oestrous cycle and early pregnancy. p19 associates strongly with the acellular capsule that surrounds the young horse conceptus and is believed to be important in maintaining pregnancy. Here we report the complete cDNA sequence encoding p19, its expression patterns in horse tissues and a Southern blot analysis of the gene in horse DNA. The predicted amino acid sequence of the p19 cDNA demonstrated a signal peptide of 18 residues and a mature protein of 162 resid... Read More
10
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 Permeation of small molecules into the cavity of ferritin as revealed by proton nuclear magnetic resonance relaxation.
The Biochemical journal
April 1, 1995
Volume 307 ( Pt 1), Issue Pt 1 253-256 doi: 10.1042/bj3070253
Yang D, Nagayama K.The NMR relaxation technique was used to investigate the permeation of molecules into the cavity of ferritin. Spin-lattice relaxation times in the rotating frame of various probe molecules were measured for solutions of recombinant horse L-apoferritin without iron and horse spleen apoferritin with very small amounts of ferric ions. The results show that molecules larger than the size of the ferritin channels can pass through the channels into the ferritin interior, and that the maximum size of molecules for the permeation is smaller than maltotriose. Characterization of a novel Na+-independent amino acid transporter in horse erythrocytes.
The Biochemical journal
April 1, 1985
Volume 227, Issue 1 13-20 doi: 10.1042/bj2270013
Fincham DA, Mason DK, Young JD.Horse erythrocytes are polymorphic with respect to L-alanine permeability. The present investigation compared the specificity, kinetics and cation-dependence of erythrocyte amino acid transport in two groups of thoroughbred horses, those with erythrocyte L-alanine permeabilities in the range 5-15 mumol/h per litre of cells (0.2 mM extracellular L-alanine, 37 degrees C) (transport-negative type) and those with L-alanine permeabilities in the range 450-700 mumol/h per litre of cells (transport-positive type). Transport-positive cells are shown to possess a novel high-affinity, stereospecific, Na... Horse liver alcohol dehydrogenase. A study of the essential lysine residue.
The Biochemical journal
September 1, 1975
Volume 149, Issue 3 627-635 doi: 10.1042/bj1490627
Chen SS, Engel PC.1. The inactivation of horse liver alcohol dehydrogenase by pyridoxal 5'-phosphate in phosphate buffer, pH8, at 10 degrees C was investigated. Activity declines to a minimum value determined by the pyridoxal 5'-phosphate concentration. The maximum inactivation in a single treatment is 75%. This limit appears to be set by the ratio of the first-order rate constants for interconversion of inactive covalently modified enzyme and a readily dissociable non-covalent enzyme-modifier complex. 2. Reactivation was virtually complete on 150-fold dilution: first-order analysis yielded an estimate of the r... A novel horse alpha-defensin: gene transcription, recombinant expression and characterization of the structure and function.
The Biochemical journal
July 11, 2007
Volume 407, Issue 2 267-276 doi: 10.1042/BJ20070747
Bruhn O, Regenhard P, Michalek M, Paul S, Gelhaus C, Jung S, Thaller G, Podschun R, Leippe M, Grötzinger J, Kalm E.Defensins are a predominant class of antimicrobial peptides, which act as endogenous antibiotics. Defensins are classified into three distinct sub-families: theta-, beta-, and alpha-defensins. Synthesis of alpha-defensin has been confirmed only in primates and glires to date and is presumably unique for a few tissues, including neutrophils and Paneth cells of the small intestine. Antimicrobial activities of these peptides were shown against a wide variety of microbes including bacteria, fungi, viruses and protozoan parasites. In the present study, we report the characterization of the equine a... 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 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 Amino acid sequence of HSP-1, a major protein of stallion seminal plasma: effect of glycosylation on its heparin- and gelatin-binding capabilities.
The Biochemical journal
September 1, 1995
Volume 310 ( Pt 2), Issue Pt 2 615-622 doi: 10.1042/bj3100615
Calvete JJ, Mann K, Schäfer W, Sanz L, Reinert M, Nessau S, Raida M, Töpfer-Petersen E.We report the complete amino acid sequence of HSP-1, a major protein isolated from stallion seminal plasma or acid extracts of ejaculated spermatozoa. The protein consists of 121 amino acids organized in two types of homologous repeats arranged in the pattern AA'BB'. Each of the 13-15-residue A-type repeats contains two O-linked oligosaccharide chains. The B-type repeats span 44-47 amino acids each, are not glycosylated, and have the consensus pattern of the gelatin-binding fibronectin type-II module. This domain also occurs in the major bovine seminal plasma heparin-binding proteins PDC-109 (... Isolation and some molecular parameters of elastase-like normal proteinases from horse blood leucocytes.
The Biochemical journal
February 1, 1976
Volume 153, Issue 2 389-396 doi: 10.1042/bj1530389
Dubin A, Koj A, Chudzik J.Cytoplasmic granules were isolated from horse blood polymorphonuclear leucocytes by the heparin method and extracted with 0.9% NaCl by repeated freezing. Soluble proteins were separated on a column of Sephadex G-75 followed by chromatography on a column of CM-Sephadex with a NaCl gradient. Gel filtration, density-gradient centrifugation, isoelectric focusing and 0.1% sodium dodecyl sulphate/polyacrylamide-gel electrophoresis at pH 7.0 and at pH 4.5 were used to determine molecular parameters of proteinases. Three enzymes hydrolysing both casein and N-benzyloxycarbonyl-L-alanine nitrophenyl est... Differences between horse and human haemoglobins in effects of organic and inorganic anions on oxygen binding.
The Biochemical journal
March 15, 1990
Volume 266, Issue 3 897-900
Giardina B, Brix O, Clementi ME, Scatena R, Nicoletti B, Cicchetti R, Argentin G, Condo SG.Despite the fact that the horse is one of the more common domesticated animals, there are few reports dealing with the properties of its blood, and no comprehensive study has been performed on the reactivity of horse haemoglobin towards organic and inorganic ions. Here we report data on the effects of the organic phosphates D-glycerate-2,3-bisphosphate (2,3-DPG) and InsP6, and of chloride on the properties of horse haemoglobin. Thus the effect of saturating concentrations of 2,3-DPG on the oxygen affinity of horse haemoglobin is about 60% lower than with human adult haemoglobin under the same ... 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