Omneity® Pellets
All-In-One Vitamin & Mineral Pellet
European journal of biochemistry
Discontinued
Publisher:
Springer.. Oxford, UK : Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies (2004)
Frequency: Twenty four no. a year
Country: England
Language: English
Author(s):
Federation of European Biochemical Societies.
Start Year:1967 - 2004
ISSN:
0014-2956 (Print)
1432-1033 (Electronic)
0014-2956 (Linking)
1432-1033 (Electronic)
0014-2956 (Linking)
Impact Factor
5.622
2021
| NLM ID: | 0107600 |
| (DNLM): | E15940000(s) |
| (OCoLC): | 01568454 |
| Coden: | EJBCAI |
| Classification: | W1 EU68 |
Stabilization of the C-terminal part of pig and horse colipase by carboxypeptidase and trypsin inhibitors. Pig and horse colipases have been purified by a common procedure using trypsin and carboxypeptidase inhibitors as stabilizers. Two forms of pig colipase were identified: a predominant A1 form with about 103-105 residues, and a minor slightly degraded A2 form in which the last two C-terminal residues, Asp and Ser, were lacking. This type of degradation is considerably slowed down by carboxypeptidase inhibitors. A total of four forms of the horse cofactor were characterized: two (A1 and B1) were probably isocolipases which differed by only a few substitutions. Both contained the same number of r...
Differences in the interactions of liver alcohol dehydrogenases with probes binding into the substrate pocket. The interactions of three groups of probes (berberine alkaloids, tricyclic psychopharmaca and acridine derivatives) with isoenzymes of horse liver alcohol dehydrogenase and with rat liver alcohol dehydrogenase have been examined. These compounds inhibit the activity of the EE isoenzyme of horse liver alcohol dehydrogenase but differ in their behaviour towards the steroid-active enzymes (i.e. the ES isoenzyme of horse liver alcohol dehydrognase and alcohol dehydrogenase from rat liver): psychopharmaca inhibit, acridines activate and berberines do not bind. The ligands differ also in their influ...
Circular dichroic properties and conformation of thionicotinamide dinucleotides bound to horse-liver alcohol dehydrogenase. The interaction between horse liver alcohol dehydrogenase and the oxidized and reduced forms of the 3-thionicotinamide--adenine dinucleotide coenzyme analogues (sNAD and sNADH) has been investigated by ultraviolet absorption, fluorescence and circular dichroism. The fluorescence of sNADH is enhanced when bound to the enzyme, and the protein fluorescence is quenched by both sNADH (60--65%) and sNAD (65%). The possible origin of the larger quenching produced by sNAD with respect to that of NAD is discussed. Coenzyme dissociation constants have been determined by monitoring the quenching of the p...
Horse-liver alcohol dehydrogenase and Pseudomonas testosteroni 3(17)beta-hydroxysteroid dehydrogenase transfer epimeric hydrogens from NADH to 17beta-hydroxy-5alpha-androstan-3-one. An exception to one of the Alworth-Bentley rules. In the reduction of 17beta-hydroxy-5alpha-androstan-3-one to the 3beta-alcohol, horse liver alcohol dehydrogenase utilizes the 4-pro-R hydrogen of NADH whereas the 3(17)beta-hydroxysteroid dehydrogenase of Pseudomonas testosteroni utulized the 4-pro-S hydrogen. These observations provide an exception to the rule proposed by Alworth and Bentley that with regard to the paired methylene hydrogens at C-4 of NADH and NADPH "the stereospecificity of a particular reaction is fixed and does not vary with the source of the enzyme preparation". It is also apparent that for these two enzymes, the selecti...
Chemical modification as a probe of the topography and reactivity of horse-spleen apoferritin. In apoferritin, but not in ferritin, 1.0 +/- 0.1 cysteine residue per subunit can be modified. In ferritin 3.3 +/- 0.3 lysine residues and 7.1 +/- 0.7 carboxyl groups per subunit can be modified, whilst the corresponding values for apoferritin are 4.4 +/- 0.4 lysine residues and 11.0 +/- 0.4 carboxyl groups per subunit. Modification of lysine residues which maleic anhydride and carboxyl groups with glycineamide in apoferritin which has been dissociated and denatured in guanidine hydrochloride leads to the introduction of 9.1 +/- 0.5 maleyl groups per subunit and 22.0 +/- 0.9 glycineamide resid...
Conformational studies of equilibrium structures in fragments of horse heart cytochrome c. Ultraviolet absorption and circular dichroism studies have been carried out on horse heart apo-cytochrome c and heme-free peptide fragments obtained by cyanogen bromide cleavage of the native protein. It was noted that the various peptides assume predominantly an unordered conformation in water solution. Increasing ionic strength and addition of 2-chloroethanol increase the right-handed helical content. Guanidinium hydrochloride favors the coil state. It was also demonstrated that two non-interacting helical regions of different stability are present in the apo-protein in 2-chloroethanol.
Cytochrome c: a thermodynamic study of the relationship among oxidation state, ion-binding and structural parameters. Cation binding to horse-heart ferrocytochrome c. The specific binding of cations to horse heart ferrocytochrome c has been studied, using the gel
filtration method. The cations investigated were: Mg2+, Co2+, cinchonine and proflavine. The stability
constants are in the range of 5-8 mM-1, and the number of binding sites per protein molecule are
1 to 2. The temperature dependence of the stability constant for the Mg2+-ferrocytochrome system
was measured. The thermodynamic parameters were found to be: dH&s = 4-12 kcal/mol, dG;,,
(25 "C) = -5.6 kcal/mol and AS&, = +57 calxmol-lx K-I.
Occurrence and nature of equine and bovine myoglobin dimers. In commercial samples of equine myoglobin and samples of equine and bovine myoglobin prepared in the laboratory, a small amount of the protein was present as an aggregate. The presence of the myoglobin aggregate could be demonstrated by gel filtration on Sephadex G-100 Superfine, which also provided a means of isolating it. Gel filtration on Sephadex G-100 showed the molecular weights of the equine and bovine moyglobin aggregates to be about 35000 and 34000 respectively, thus supporting the hypothesis that they are dimers. This was confirmed for the equine myoglobin by ultracentrifugation meas...
Binding of long chain alkyl sulphates to equine ferric myoglobin. When ferric myoglobin reacts with alkyl sulphates, its absorption spectrum changes into one characteristic of a haemichrome or parahaematin. The reaction equilibrium was studied over a range of protein concentrations using dodecyl sulphate and other alkyl sulphates with different chain lengths. The results obtained from spectrophotometric measurements and equilibrium dialysis experiments are not in agreement with those of other authors who, from an analysis of spectral changes only, supported the hypothesis of an all-or-none type of reaction whereby 18 detergent anions were bound to one molecu...
