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Biomedical subjects

Z Zak

Publications and source records attributed to Z Zak.

At least 19 recordsLinked to original sources
PubMed2006

Novel cation [N(SO2NMe3)2]+ and its synthesis and crystal structure. Dichloride of imido-bis(sulfuric) acid HN(SO2Cl)2. Part 1. Crystal structures of KN(SO2Cl)2.(1/2)CH3CN, KN(SO2Cl)2.(1/6)CH2Cl2, and [PCl4][N(SO2Cl)2].

Several salts of bis(chlorosulfonyl)imide HN(SO2Cl)2 (1), namely, two solvates of its potassium salt, KN(SO2Cl)2.(1/2)CH3CN (1K1), KN(SO2Cl)2.(1/6)CH2Cl2 (1K2), and its tetrachlorophosphonium salt, [PCl4][N(SO2Cl)2] (2), were prepared and structurally characterized. The reaction of HN(SO2Cl)2 with Me3N gives the [N(SO2Cl)2]- salt of a novel cation, [N(SO2NMe3)2]+. This cation is analogous to the [HC(SO2NMe3)2]+ cation, but in contrast to the latter, it is fairly stable to hydrolysis. The salt [N(SO2NMe3)2]+[N(SO2Cl)2]- (3) can be converted into salts of other anions by being treated with diluted aqueous solutions of the respective acids, and thus NO3-, Cl-.H2O, SeO3(2-), CH3COO-, HSO4-, (COO)2(2-) salts were prepared. Treatment of 3 with concentrated HNO3 gave the [N(SO2NMe3)2]+ [O2NO-H-ONO2]- salt, and the addition of an HCl-acidified FeCl3 aqueous solution yielded the FeCl4- salt. Methanolysis resulted in the formation of MeOSO3- and [MeOSO2NSO2OMe]- salts. All salts have been characterized by chemical analysis, vibrational spectroscopy, and X-ray structure determinations.

Journal Article↗
PubMed1995

Treatment with beta-adrenergic blocking agents after myocardial infarction: from randomized trials to clinical practice.

OBJECTIVES: Our aim was to determine the percent of patients with myocardial infarction who are treated with beta-adrenergic blocking agents in dosages proved to be effective in preventing death after a heart attack. BACKGROUND: In the prospective randomized trials showing that beta-blocker treatment improves survival rates after myocardial infarction, relatively high dosages of these agents were used. However, it is not known whether these dosages are used in current clinical practice. METHODS: In a retrospective analysis of clinical data from 606 consecutive survivors of myocardial infarction at four university hospitals in three countries, we assessed the number of infarct survivors receiving prospectively defined "effective dosages" of beta-blockers. We defined these dosages as those that demonstrated improved survival rates of infarct survivors who received active drug in large, prospective, double-blind, placebo-controlled trials. RESULTS: Only 58% of infarct survivors with no contraindications to beta-blockers received these drugs at the time of hospital discharge, and only 11% received dosages equivalent to > 50% of the effective dosages. Independent predictors of failure to prescribe beta-blockers to infarct survivors without contraindications to these drugs were the use of diuretic agents, transient heart failure, impaired left ventricular function and increased patient age. Among patients receiving beta-blockers, only the use of propranolol predicted prescription of a low beta-blocker dosage. CONCLUSIONS: Failure to prescribe beta-blockers after myocardial infarction is common but in most cases is not due to clear contraindications. Many patients not receiving beta-blockers belong to subgroups that would derive the greatest benefit from such treatment. Finally, even when beta-blockers are prescribed, the dosages used are considerably lower than those proved to be effective in preventing death after myocardial infarction.

Adrenergic beta-Antagonists↗
PubMed1993

Fluorescence quenching in riboflavin-binding protein and its complex with riboflavin.

Fluorescence quenching of tryptophan residues in egg-white riboflavin-binding protein by two typical quenchers (charged iodide and uncharged acrylamide) reveals acid-induced changes of protein conformation. At neutral pH, acrylamide flow in macromolecule, (i.e., the quenching effect) is decisive; tryptophan residue accessibility for iodide is small. At low pH, some tryptophan residues are exposed to the protein surface and become more accessible to iodide. In contrast, acrylamide is less able to permeate this conformational state of RBP. Fluorescence of tryptophan residues in riboflavin-RBP complex and chemically N-bromosucinimide-modified RBP was quenched by iodide and acrylamide.

Acrylamides↗
PubMed1991

Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Spectral properties of wild type and mutated enzymes.

Three amino acid residues in the active site of lipoamide dehydrogenase from Azotobacter vinelandii were replaced by other residues. His450, the active-site base, was changed into Ser, Tyr and Phe. Pro451, in cis conformation, was changed into Ala. Glu455 was replaced with Asp and Gln. Absorption, fluorescence and CD spectroscopy of the mutated enzymes in their oxidized state (Eox) showed only minor changes with respect to the wild-type enzyme, whereas considerable changes were observed in the spectra of the two-electron-reduced (EH2) species of the enzymes upon reduction by the substrate dihydrolipoamide. Differences in extent of reduction of the flavin by NADH indicate that the redox potential of the flavin is altered by the mutations. Enzyme Pro451----Ala [corrected] showed the greatest deviation from wild type. The enzyme is very easily over-reduced to the four-electron reduced state (EH4) by dihydrolipoamide. This is probably due to a change in the backbone conformation caused by the cis-trans conversion. From studies on the pH dependence of the thiolate charge-transfer absorption and the relative fluorescence of EH2 of the enzymes, it is concluded that mutation of His450 results in a relatively simple and easily interpreted distribution of electronic species at the EH2 level. For all three His450-mutated enzymes an apparent pKa1 near 5.5 is calculated that is assigned to the interchange thiol. A second apparent pKa2 is calculated of 6.9, 7.5 and 7.1 for the His450----Phe, -Ser and -Tyr enzymes, respectively, and signifies the deprotonation of the tautomeric equilibrium between the interchange and charge-transfer thiols. The difference in apparent pKa2 values between the His450-mutated enzymes is explained by changes in micropolarity. At the EH2 level the wild-type enzyme consists of multiple electronic forms as reported for the Escherichia coli enzyme [Wilkinson, K. D. and Williams C. H. Jr (1979) J. Biol. Chem. 254, 852-862]. Based on the results obtained with the His450-mutated enzymes, it is concluded that the lowest pKa is associated with the interchange thiol. A model for the equilibrium species of the wild-type enzyme at the EH2 level is presented which takes three pKa values into account. The results of the pH dependence of the electronic species at the EH2 level of Glu455-mutated enzymes essentially follow the model proposed for the wild-type enzyme. However mutation of Glu455 shifts the tautomeric equilibrium of EH2 in favor of the charge-transfer species.(ABSTRACT TRUNCATED AT 400 WORDS)

Azotobacter vinelandii↗
PubMed1990

Purification and properties of chicken egg-white cobalamin-binding protein.

A cobalamin-binding protein has been purified from chicken egg-white by using a combination of conventional and high performance ion-exchange chromatography. Following initial purification by DEAE-cellulose, ammonium sulphate precipitation, Sephacryl S-200 CM-cellulose and affinity chromatography, appropriate fractions were further purified using the Pharmacia fast protein liquid chromatography (FPLC) system. Using this method of purification, egg-white CBP has been purified more rapidly and with greater recovery than with conventional column chromatography. The homogeneity of this protein was verified by SDS-PAGE. The Mr was 37,000 by SDS-PAGE and 39,000 by gel filtration, which indicated that it was a glycoprotein. The stokes radius was 4.1 nm and pI was 4.3. The protein bound 57COB12 with a molar ratio of 1/1 and kd of 0.40 microM. The egg-white CBP was composed of 294 amino acid residues. Thiol groups and metal ions were not connected with the Cbl-binding activities.

Amino Acid Sequence↗
PubMed1989

Purification and partial characterization of a cobalamin-binding protein from chicken egg yolk.

Cobalamin-binding protein has been purified from chicken egg yolk by using DEAE-cellulose with a NaCl gradient. The resultant protein fraction was subjected to bioaffinity chromatography. The Mr was 38,000 by SDS-PAGE and 39,000 by gel filtration, and indicated that it was a glycoprotein. The Stokes radius was 4.3 nm and the pI 4.1. The protein bound 57CO.B12 with a molar ratio of 1:1 and a Kd of 0.41 microM. The CBP composed 296 amino acids residues. The protein-ligand interaction was inhibited by Cbl analogues.

Amino Acids↗
PubMed1989

Affinity chromatographic identification of vitamin B12-binding proteins in egg white.

To identify vitamin B12-binding proteins in egg white, an affinity chromatographic isolation procedure was applied. A fraction tightly absorbed on vitamin B12 immobilized in agarose was eluted with 1 mM cyanocobalamin, and then separated by isoelectric focusing in sucrose density gradient. Two isolated proteins (or perhaps two forms of the same protein) of isoelectric points 6.2 and 7.2 and the same Mr 90,000 were found capable of detectable vitamin B12 binding. They are probably glycoproteins, each composed of a single polypeptide chain.

Animals↗
PubMed1988

1,2-Cyclohexanedione modification of arginine residues in egg-white riboflavin-binding protein.

1. Reaction of 1,2-cyclohexanedione with arginine residues of egg white riboflavin-binding protein results in a loss of the binding activity. 2. In borate buffer pH 8.0, with 0.15 M cyclohexanedione, the inactivation proceeds with a pseudo-first-order rate constant 0.084 hr.-1. 3. At least 65% of lost riboflavin binding capacity can be recovered on 12 hr incubation in 0.5 M hydroxylamine pH 7.0. 4. All 5 arginine residues are modified, 2-3 of them seem to react much easier than others. 5. The correlation between modification of arginines and protein inactivation, as analyzed by kinetic and statistical methods, suggests that one of low-reactivity residues is "essential" for riboflavin binding. 6. In the holoprotein, one arginine residue is almost completely protected from 1,2-cyclohexanedione modification. 7. Riboflavin does not dissociate from holoprotein, even on prolongated incubation with the reagent. 8. The protected arginine residue seems to be located in the riboflavin binding pocket of protein macromolecule.

Arginine↗
PubMed1987

The effect of riboflavin binding protein (RPB) on flavokinase catalytic activity.

1. Flavokinase isolated from 18-day chick embryo liver shows optimal activity at pH 8.6, in the presence of the divalent cations Zn2+, Ca2+ and Mn2+. 2. The activity and stability of flavokinase depends on the RBP concentration. 3. Interaction between flavokinase and riboflavin binding protein was demonstrated by means of crossed immunoelectrophoresis and affinity chromatography.

Animals↗
PubMed1982

Distribution and properties of flavokinase in the developing chick embryo.

1. Localization of flavokinase was studied in the nonembryonic portions of the chicken egg, in embryos at various stages of development, and in the adult hen. 2. Embryonic biosynthesis of flavin nomonucleotide (FMN) increases with increasing protein synthesis. 3. In the embryo, higher activity of flavokinase was observed in intestine, heart, liver, and yolk sac. 4. Lower activity was observed in allantoic membrane and fluid. 5. No significant activity was measured in yolk. 6. Both specific and total flavokinase activities in organs of the more aerobic and metabolically active adult chicken are considerably greater than those of embryo organs. 7. Flavokinase from embryonic liver was enriched by affinity chromatography by using N-10-flavinyl agarose. 8. The partially purified enzyme has properties generally similar to other animal flavokinases.

Animals↗
PubMed1976

Effect of antibody on interaction between vitamin B2 and riboflavin apoprotein.

1. Dissociation of riboflavin from flavoprotein and from the flavoprotein-antibody complex occurs under the same conditions. 2. The precipitated apoprotein-antibody complex retains 15% of the apoprotein capacity to bind riboflavin. After solubilization of the complex in 0.3 M-KCl or 1 M-urea, the binding of riboflavin amounts to 80 - 90% of its capacity. 3. The apoprotein modified by oxidation of 50% of tryptophan residues loses the ability to bind riboflavin but its immunological reactivity with the anti-flavoprotein antibody is similar to that of native apoprotein. The apoprotein with all tryptophan residues oxidized shows much lower immunoreactivity. 4. The obtained results suggest that in riboflavin flavoprotein the region around the riboflavin-binding site does not show the properties of an antigenic determinant.

Animals↗