Analyze Diet

Biochimica et biophysica acta.

Discontinued
Periodical
Biochemistry
Biophysics
Publisher:
Elsevier Pub. Co.
Frequency: One hundred issues per year, 2006-
Country: Netherlands
Language: English
Start Year:1947 - 2016
ISSN:
0006-3002 (Print)
1878-2434 (Electronic)
0006-3002 (Linking)
Impact Factor
6.2
2022
NLM ID:0217513
(OCoLC):01536398
(DNLM):B15340000(s)
Coden:BBACAQ
LCCN:49048142
Classification:W1 BI652
Circular dichroism study of horse colipase interaction with bile salt.
Biochimica et biophysica acta    October 28, 1981   Volume 670, Issue 3 305-311 doi: 10.1016/0005-2795(81)90101-x
Canioni P, Julien R, Romanetti R, Cozzone P, Sarda L.No abstract available
Mobilization of iron from ferritin by isolated mitochondria. Effects of species compatibility between ferritin and mitochondria and iron content of ferritin.
Biochimica et biophysica acta    September 18, 1981   Volume 677, Issue 1 50-56 doi: 10.1016/0304-4165(81)90144-6
Ulvik RJ, Romslo I, Roland F, Crichton RR.Mitochondria mobilize iron from ferritin by a mechanism that depends on external FMN. With rat liver mitochondria, the rate of mobilization of iron is higher from rat liver ferritin than from horse spleen ferritin. With horse liver mitochondria, the rate of iron mobilization is higher from horse spleen ferritin than from rat liver ferritin. The results are explained by a higher affinity between mitochondria and ferritins of the same species. The mobilization of iron increases with the iron content of the ferritin and then levels off. A maximum is reached with ferritins containing about 1 200 i...
Electron transfer between horse heart and Candida krusei cytochromes c in the free and bound states.
Biochimica et biophysica acta    July 1, 1981   Volume 636, Issue 2 129-135 doi: 10.1016/0005-2728(81)90085-2
Yoshimura T, Sogabe T, Aki K.Electron transfer between horse heart and Candida krusei cytochromes c in the free and phosvitin-bound states was examined by difference spectrum and stopped-flow methods. The difference spectra in the wavelength range of 540-560 nm demonstrated that electrons are exchangeable between the cytochromes c of the two species. The equilibrium constants of the electron transfer reaction for the free and phosvitin-bound forms, estimated from these difference spectra, were close to unity at 20 degrees C in 20 mM Tris-HCl buffer (pH 7.4). The electron transfer rate for free cytochrome c was (2-3).10(4)...
Amino acid sequence of horse colipase B.
Biochimica et biophysica acta    June 29, 1981   Volume 669, Issue 1 39-45 doi: 10.1016/0005-2795(81)90221-x
Bonicel J, Couchoud P, Foglizzo E, Desnuelle P, Chapus C.The complete sequence of the 96 residues composing horse colipase B has been determined by automated analysis of the intact protein, of two CNBr peptides and two tryptic peptides arising, respectively, from the citraconylated chain and from the unreduced protein. The single histidine of the protein is located at position 29 as in horse colipase A. His86, present in the C-terminal region of the pig cofactor and supposed to play a role in the folding molecule, is not conserved in horse B. Large pieces of the pig and horse B chains were found to be identical or very similar, especially the N-term...
Nucleic acid-protein interactions. Degradation of double-stranded RNA by glycosylated ribonucleases.
Biochimica et biophysica acta    June 26, 1981   Volume 654, Issue 1 77-85 doi: 10.1016/0005-2787(81)90138-6
Carsana A, Furia A, Gallo A, Beintema JJ, Libonati M.1. Extensively glycosylated ribonucleases, like the enzymes from pig and horse pancreas, show a much higher activity on double-stranded RNAs than similarly charged, carbohydrate-free RNAases under stranded assay conditions (relatively high salt concentrations). Glycosylated pig and horse pancreas RNAases also show a larger destabilizing effect on double-stranded poly[d(A-T)] X poly[d(A-T)], than that displayed by bovine RNAase A under these conditions. Both activities show a similar dependence on the ionic strength of the medium. 2. A partial enzymic removal of the heterosaccharide side chains...
Physico-chemical properties of pregnant mare serum gonadotropin.
Biochimica et biophysica acta    February 27, 1981   Volume 667, Issue 2 267-276 doi: 10.1016/0005-2795(81)90192-6
Combarnous Y, Salesse R, Garnier J.Pregnant mare serum gonadotropin exhibits a dissociation at acid pH as shown by the drop of s20,w values from 3.52 S at pH 8.1 to 2.52 S at pH 2.0. The dissociation is accompanied by an absorbance change with a maximum at 287 nm and a parallel loss of both follicle-stimulating hormone (FSH) and luteinizing hormone (LH) activities as followed by radioreceptor assays. The apparent pKa of the acid transition is 3.45 with an extremely slow and temperature-dependent rate at pH 2.0 (1.8 . 10(-4) s-1 at 37 degrees C). By gel filtration the molecular weight of the active hormone is estimated to be 45 ...
Activation of pigeon erythrocyte adenylate cyclase by cholera toxin. Partial purification of an essential macromolecular factor from horse erythrocyte cytosol.
Biochimica et biophysica acta    February 5, 1981   Volume 672, Issue 3 248-261 doi: 10.1016/0304-4165(81)90291-9
Le Vine H, Cuatrecasas P.A cytosolic, macromolecular factor required for the cholera toxin-dependent activation of pigeon erythrocyte adenylate cyclase and cholera toxin-dependent ADP-ribosylation of a membrane-bound 43,000 dalton polypeptide has been purified 1100-fold from horse erythrocyte cytosol using organic solvent precipitation and heat treatment. This factor, 13,000 daltons, does not absorb to anionic or cationic exchange resins, is sensitive to trypsin or 10% trichloroacetic acid and is not extractable by diethyl ether. Activation of adenylate cyclase by cholera toxin requires the simultaneous presence of AT...
Fractionation and partial characterization of alpha-1-protease isoinhibitors of horse.
Biochimica et biophysica acta    December 4, 1980   Volume 616, Issue 2 351-361 doi: 10.1016/0005-2744(80)90152-7
Pellegrini A, von Fellenberg R.The principal alpha-1-protease inhibitor of horse was fractionated by classical methods and analysed with a modified fibrinogen-agarose gel electrophoretic method of high sensitivity and resolving power. Starting with an electrophoretically homogeneous inhibitor in unfractionated serum, two isoinhibitor bands became apparent after fractionation with (NH4)2SO4 and DEAE-cellulose DE-52 ion-exchange chromatography. The isoinhibitors differed in electrophoretic migration and in the elution pattern from Sephadex G-100 gel filtration, but possessed identical antigenic determinants and enzyme specifi...
Identification by gas-liquid chromatography-mass spectrometry of 4-O-acetyl-9-O-lactyl-N-acetyl-neuraminic acid, a new sialic acid from horse submandibular gland.
Biochimica et biophysica acta    June 19, 1980   Volume 630, Issue 2 306-310 doi: 10.1016/0304-4165(80)90435-3
Reuter G, Pfeil R, Kamerling JP, Vliegenthart JF, Schauer R.The novel sialic acid 4-O-acetyl-9-O-lactyl-N-acetylneuraminic acid has been identified as a constituent of horse submandibular gland glycoproteins in addition to the already known equine sialic acids, N-acetylneuraminic acid, 4-O-acetyl-N-acetylneuraminic acid, 9-O-acetyl-N-acetylneuraminic acid, 4,9-di-O-acetyl-N-acetylneuraminic acid, N-glycolylneuraminic acid, 4-O-acetyl-N-glycolylneuraminic acid and 9-O-acetyl-N-glycolylneuraminic acid. The structure has been established by combined gas-liquid chromatography-mass spectrometry.
The effect of trypsin digestion on the structure and iron-donating properties of transferrins from several species.
Biochimica et biophysica acta    April 25, 1980   Volume 622, Issue 2 297-307 doi: 10.1016/0005-2795(80)90040-9
Esparza I, Brock JH.The effect of trypsin digestion on iron-saturated and iron-free (apo) human, rabbit, bovine, pig and horse tranferrins has been studied. Iron-binding fragments were produced only from iron-saturated pig and bovine transferrins although some cleavage of the polypeptide chain occurred in all cases. The apo-transferrins were generally degraded to a greater extent than the corresponding iron-saturated proteins. The ability of the different transferrins to donate iron to rabbit reticulocytes varied in the order rabbit approximately pig greater than human approximately horse greater than bovine. Try...
Purification by affinity chromatography and characterization of a neutral alpha-glucosidase from horse kidney.
Biochimica et biophysica acta    March 14, 1980   Volume 612, Issue 1 85-96 doi: 10.1016/0005-2744(80)90281-8
Giudicelli J, Emiliozzi R, Vannier C, de Burlet G, Sudaka P.A horse kidney neutral alpha-D-glucosidase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20) was purified about 580-fold with a yield of 33% by an affinity chromatography technique using the p-aminophenyl-beta-D-maltoside, a substrate derivative, as ligand. The purified enzyme, homogeneous in polyacrylamide gel electrophoresis, was a glycoprotein with a molecular weight of 280 000 as calculated by gel filtration and its isoelectric focusing points was found to be pH 4.1. The purified enzyme was able to hydrolyze various substrates having (alpha-1,2), (alpha-1,3), (alpha-1,4), and (alpha-1,6) glu...
Occurrence of Leu-Lys-bradykinin and histidine-rich peptide in high-molecular-weight kininogen isolated from horse plasma.
Biochimica et biophysica acta    August 28, 1979   Volume 579, Issue 2 474-478 doi: 10.1016/0005-2795(79)90076-x
Sugo T, Kato H, Iwanaga S, Fujii S.On incubation of purified horse plasma high-molecular-weight kininogen with purified plasma kallikrein, three new peptides, named fragment 1.2, fragment 1 and fragment 2, were released, in addition to the vasopeptide, bradykinin. Fragment 2 contained an extremely high level of histidine, in which eleven residues out of the total 48 residues were characterized. Thus the result proves the existence of the histidine-rich region in horse high-molecular-weight kininogen, which is similar to the region previously identified in bovine high-molecular-weight kininogen. Moreover, we have identified a ne...
A mechanistic model for butyrylcholinesterase.
Biochimica et biophysica acta    March 16, 1979   Volume 567, Issue 1 161-173 doi: 10.1016/0005-2744(79)90183-9
Eriksson H, Augustinsson KB.A plausible mechanism of action of horse serum butyrylcholinesterase is proposed. It includes substrate activation at the level of deacylation. The rate constant for the acylation of the enzyme appears to be much greater than the rate constant for the deacylation, at low substate concentrations. At higher substrate concentrations the rate constants become more similar. No interaction between the four subunits in binding of inhibitors or in the catalysis was observed. There is one esteratic and one anionic site per subunit apparent from labelling studies with [32P]diisopropylfluorophosphate and...
The presence of two (Na+ + K+)-ATPase inhibitors in equine muscle ATP: vanadate nad a dithioerythritol-dependent inhibitor.
Biochimica et biophysica acta    August 4, 1978   Volume 511, Issue 2 202-212 doi: 10.1016/0005-2736(78)90314-0
Quist EE, Hokin LE.A potent inhibitor of (Na+ + K+)-ATPase activity was purified from Sigma equine muscle ATP by cation- and anion-exchange chromatography. The isolated inhibitor was identified by atomic absorption spectroscopy and proton resonance spectroscopy to be an inorganic vanadate. The isolated vanadate and a solution of V2O5 inhibit sarcolemma (Na+ + K+)-ATPase with an I50 of 1 micrometer in the presence of 1 mM ethyleneglycol-bis-(beta-aminoethylether)-N,N'-tetraacetic acid (EGTA), 145 mM NaCl, 6mM MgCl2, 15 mM KCl and 2 mM synthetic ATP. The potency of the isolated vanadate is increased by free Mg2+. ...
Physicochemical and biological characterizations of pregnant mare serum gonadotropin and its subunits.
Biochimica et biophysica acta    January 25, 1978   Volume 532, Issue 1 185-194 doi: 10.1016/0005-2795(78)90462-2
Papkoff H, Bewley TA, Ramachandran J.Pregnant mare serum gonadotropin and its subunits have been further characterized. Ultracentrifugation of the gonadotropin at pH 1.3 and 11.5 showed little evidence of dissociation compared to pH 8.2. Highly purified subunits are obtained by urea dissociation and ion-exchange chromatography followed by gel-filtration. Circular dichroism spectra of the gonadotropin and its subunits are much like those of ovine lutropin and its subunits in that there is little evidence for secondary structure and one or more tyrosine residues are inaccessible in the intact gonadotropin compared to the subunits. ...
Circular dichroism of porcine, bovine, and equine pancreatic phospholipases A2 and their zymogens. Unusual conformations simulating helix content.
Biochimica et biophysica acta    October 26, 1977   Volume 494, Issue 2 285-292 doi: 10.1016/0005-2795(77)90157-x
Jirgensons B, de Haas GH.Conformation of porcine, bovine, and equine pancreatic phospholipases A2 (EC 3.1.1.4) and their zymogens was studied by the circular dichroism (CD) probe in the far and near ultraviolet spectral zones. All these phospholipases and their zymogens displayed CD curves suggesting the presence of moderate amounts of α-helical conformation. However, on the basis of known primary structure and recent X-ray structural analysis of prophospholipase A2 crystals (Drenth, J., Enzing, C.M., Kalk, K.H. and Vessies, J.C.A. (1976) Nature 264, 373–377), it has to be concluded that the positive CD band cen...
Isolation and properties of prophospholipase A2 and phospholipase A2 from horse pancreas and horse pancreatic juice.
Biochimica et biophysica acta    March 28, 1977   Volume 491, Issue 1 265-274 doi: 10.1016/0005-2795(77)90062-9
Evenberg A, Meyer H, Verheij HM, de Haas GH.Two phospholipases A2 (EC 3.1.1.4) with different isoelectric points have been isolated from horse pancreas in high yield (880 mg/kg tissue). From pancreatic juice the more acidic species was isolated as the sole phospholipase A2. Upon tryptic activation the zymogens release a hepta- and pentapeptide, respectively from the N-terminal part of the protein giving rise to the formation of one single enzyme with a specific activity higher than that of pancreatic phospholipases A2 from other mammalian species. Horse phospholipase A2 differs from the porcine and bovine enzymes with respect to amino a...
Alkali-labile oligosaccharides from glycoproteins of different erythrocyte and milk fat globule membranes.
Biochimica et biophysica acta    September 7, 1976   Volume 443, Issue 3 402-413 doi: 10.1016/0005-2736(76)90460-0
Glöckner WM, Newman RA, Dahr W, Uhlenbruck G.Phenol extraction of horse, sheep, cow, pig and human erythrocyte membranes and human milk fat globule membranes gave glycoprotein fractions, all of which were shown by gas chromatography to contain the reduced disaccharide beta-D-galactosyl (1-3)-N-acetyl-D-galactosaminital after treatment with alkaline borohydride. Cow and pig erythrocyte membrane glycoproteins were found however to contain much lower amounts than the erythrocyte membrane glycoproteins of the other species tested. After gel filtration, a tetrasaccharide was isolated from horse and sheep glycoproteins containing the disacchar...
Steady-state enzyme kinetics of the pancreatic ribonucleases from five mannalian species.
Biochimica et biophysica acta    May 13, 1976   Volume 429, Issue 3 853-859 doi: 10.1016/0005-2744(76)90331-4
Ronda GJ, Gaastra W, Beintema JJ.The kinetic parameters Km, k+2 and k+2/Km of the pancreatic ribonucleases (EC 3.1.4.22) from cow, giraffe, horse, rat and lesser rorqual have been determined, using 2',3'-cyclic cytidine monophosphate and 2',3'-cuclic uridine monophosphate as substrates. No large differences were found between the activities of the five enzymes. The relative differences between the activities of the five enzymes are mainly due to differences in the rates of hydrolysis and not to differences in the affinities for the substrates.
Characterization of protein phosphokinase activities in horse thyroid nuclei.
Biochimica et biophysica acta    March 11, 1976   Volume 429, Issue 1 163-172 doi: 10.1016/0005-2744(76)90038-3
Verhaegen M, Sand G.The distribution of protein phosphokinase (EC 2.7.1.37) activities has been established in horse thyroid nuclei. The presence of several enzyme activities has been demonstrated, two of which are clearly distinct. The first one acts on histone as substrate and is activated by cyclic AMP. Physico-chemical properties of this nuclear cyclic AMP-dependent histone kinase and of the cytosol histone kinase are different, demonstrating the absence of a contamination from the cytosol. The second enzyme acts on casein as substrate and is not stimulated by cyclic AMP POR CYCLIC GMP. The findings are consi...
Carbohydrate composition of horse spleen ferritin.
Biochimica et biophysica acta    November 10, 1975   Volume 411, Issue 1 165-167 doi: 10.1016/0304-4165(75)90295-0
Shinjyo S, Abe H, Masuda M.The carbohydrate composition of horse spleen ferritin was studied. 1 mol of the apoferritin, the protein moiety of ferritin, contains 25 mol of hexose, 3 mol of hexosamine and 10 mol of fucose. Same carbohydrate composition was detected in the apoferritin from iron rich ferritins. These results indicate that horse spleen ferritin is composed of non-identical subunits as regards its carbohydrate composition.
Isolation and partial characterization of the major glycoproteins of horse and swine erythrocyte membranes.
Biochimica et biophysica acta    October 6, 1975   Volume 406, Issue 2 206-213 doi: 10.1016/0005-2736(75)90005-x
Fujita S, Cleve H.The major glycoproteins of horse and swine erythrocyte membranes were isolated and examined chemically and immunologically. The major glycoprotein of horse erythrocyte membranes had a molecular weight of 33 000 and consisted of 46.2% protein and 53.8% carbohydrate, of which 9.4% was hexose, 10.1% hexosamine and 33.7% sialic acid. This glycoprotein was associated with activity for the infectious mononucleosis heterophile antigen. There were two different major glycoproteins in swine erythrocyte membranes. One major glycoprotein had a molecular weight of 46 200 and consisted of 34.2% protein and...
Leucocyte myosin and its location in the cell.
Biochimica et biophysica acta    August 19, 1975   Volume 400, Issue 2 222-243 doi: 10.1016/0005-2795(75)90177-4
Shibata N, Tatsumi N, Tanaka K, Okamura Y, Senda N.The intracellular location of the binding site of antibody against purified myosin prepared from equine leucocytes was investigated in neutrophils and lymphocytes by electron microscopy using peroxidase-labelled antibody method. The myosin extracted from equine leucocytes could bind skeletal muscle F-actin and the formed complex showed the biophysical and biochemical properties and electron microscopic appearance of actomyosin. On immunodiffusion, the leucocyte myosin formed a single precipitin line with its antibody prepared in rabbits. The antibody also formed single precipitin lines with my...
Inhibition of horse muscle acylphosphatase by pyridoxal 5′-phosphate.
Biochimica et biophysica acta    June 24, 1975   Volume 391, Issue 2 486-493 doi: 10.1016/0005-2744(75)90272-7
Ramponi G, Manao G, Camici G, White GF.It has been shown that horse muscle acylphosphatase is inhibited by pyridoxal 5'-phosphate and that the inhibition is pH dependent, reversible and competitive with respect to substrate binding. Spectral analysis on the EI complex demonstrates the presence of a Schiff base. Reduction of the pyridoxal 5'-phosphate-inhibited enzyme with sodium borohydride, followed by amino acid analysis, produces a diminution of the free lysine peak and the appearance of a new peak corresponding to epsilon-pyridoxyllysine. The results suggest that there is at least one NH2-lysyl residue of horse muscle acylphosp...
Comparison of the myoglobin of the zebra (Equus burchelli) with that of the horse (Equus caballus).
Biochimica et biophysica acta    May 30, 1975   Volume 393, Issue 1 201-204 doi: 10.1016/0005-2795(75)90232-9
Darbre PD, Romero-Herrera AE, Lehmann H.The tryptic and peptic peptides from the myoglobin of the zebra (Equus burchelli) have been compared with those obtained from the myoglobin of the horse (Equus caballus). No differences in the myoglobin were found between these two species.
An examination of octanol and octanal metabolism to octanoic acid by horse liver alcohol dehydrogenase.
Biochimica et biophysica acta    March 28, 1975   Volume 384, Issue 1 1-11 doi: 10.1016/0005-2744(75)90090-x
Hinson JA, Neal RA.The kinetics of the horse liver alcohol dehydrogenase (alcohol: NAD+ oxidoreductase EC 1.1.1.1) catalyzed metabolism of octanol and octanal to octanoic acid have been examined. On incubation of octanol with horse liver alcohol dehydrogenase in the presence of NAD+, NADH as well as octanal and octanoic acid were seen as the initial products. However, on continued incubation, the octanal concentration progressively decreased to where only negligible quantities were present in the incubation after 10 min. The production of NADH was biphasic. An initial phase was followed in about 2 min with a slo...
Species variability in the modification of erythrocyte surface proteins by enzymatic probes.
Biochimica et biophysica acta    March 13, 1975   Volume 382, Issue 2 181-192 doi: 10.1016/0005-2736(75)90176-5
Carraway KL, Colton DG, Shin BC, Triplett RB.Bovine and equine erythrocytes have been studied by three different surface modification techniques to investigate the accessibility of the surface components to the external medium. Lactoperoxidase labeling of equine erythrocytes results in a significant labeling of only one membrane component, a 100 000-mol.wt polypeptide corresponding to the membrane-spanning Component III of human erythrocytes. The major sialoglycoprotein of the equine erythrocyte is not labeled. This is in contradistinction to the situation for human and bovine cells, where both components are labeled. The equine membrane...
Binding of Au(CN)2- and Pt(CN)4-2- to horse liver alcohol dehydrogenase. A 35C1NMR relaxation study.
Biochimica et biophysica acta    January 23, 1975   Volume 377, Issue 1 1-8 doi: 10.1016/0005-2744(75)90279-x
Bull TE, Lindman B, Einarsson R, Zeppezauer M.The binding of Au(CN)2- and Pt(CN)4-2- ions to the coenzyme binding site of horse liver alcohol dehydrogenase (alcohol : NAD+ oxidoreductase EC 1.1.1.1) has been studied by 35C1 nuclear magnetic relaxation. Longitudinal relaxation rates were analyzed in terms of a simple model and binding constants for Au(CN)2-, Pt(CN)4-2- and C1- were estimated. From a comparison between transverse and longitudinal relaxation rates the correlation time and the quadrupole coupling constant of bound chloride ion were obtained. The quadrupole coupling constant estimated from a simple electrostatic model for chlo...
The photo-oxidation of horse heart cytochrome c and native cytochrome c2 by reaction centres from Rhodopseudomonas spheroides R26.
Biochimica et biophysica acta    April 23, 1974   Volume 347, Issue 1 1-13 doi: 10.1016/0005-2728(74)90194-7
Prince RC, Cogdell RJ, Crofts AR.No abstract available
Amino acid composition and carboxyl-terminal structure of some basic chromosomal proteins of mammalian spermatozoa.
Biochimica et biophysica acta    September 21, 1973   Volume 322, Issue 1 173-177 doi: 10.1016/0005-2795(73)90189-x
Monfoort CH, Schiphof R, Roxijn TH, Steyn-Parvè EP.No abstract available