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E Misaka

Publications and source records attributed to E Misaka.

18 recordsLinked to original sources
PubMed1988

X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method.

The molecular structure of lipoamide dehydrogenase from baker's yeast has been determined at 4.5 A resolution by molecular replacement techniques using the known structure of human erythrocyte glutathione reductase as a starting model. The enzyme crystallizes in the space group P2(1)2(1)2(1) with a = 98.6(2), b = 162.0(2), c = 69.4(2) A. There is one molecule per asymmetric unit. The enzyme is a dimeric protein of identical subunits related by a local two-fold symmetry. Comparison of the tertiary structures between glutathione reductase and the present enzyme shows that the folding is almost the same except for the N and C termini, although some slight shortening or shifting of alpha-helices was found in the electron density map. FAD molecules are found at similar positions to those of glutathione reductase. Since the amino acid residues around FAD and NAD binding sites and at the reaction centers of the two enzymes are strongly conserved, the lipoamide dehydrogenase may catalyze the opposite reaction through a similar mechanism to that proposed for glutathione reductase. The newly found C terminus is located near the edge of a deep cave at the interface between the two subunits. These additional 18 residues form a narrow entrance to the cave, in which the long chain of the dihydrolipoyl moiety of lipoate acetyltransferase will be bound.

Crystallization↗
PubMed1984

Synthesis and antiinflammatory activity of [(cycloalkylmethyl)phenyl]acetic acids and related compounds.

[(Cycloalkylmethyl)phenyl]acetic acid derivatives and related compounds were synthesized to test their antiinflammatory and analgesic activities. Some of the compounds in this series were found to have good activity in the carrageenan edema test. Among them, sodium 2-[4-[(2-oxocyclopentyl)methyl] phenyl]propionate dihydrate (15) and 2-[4-[(2-oxocyclohexylidene)methyl]phenyl]propionic acid (13b) showed potent analgesic and antiadjuvant arthritis activities with excellent antipyretic properties.

Analgesics↗
PubMed1983

Decrease of urinary prostaglandin E2 and prostaglandin F2 alpha excretion by nonsteroidal anti-inflammatory drugs in rats. Relationship to anti-inflammatory activity.

An analytical method for measuring in vivo inhibition of prostaglandin (PG) synthesis by nonsteroidal anti-inflammatory drugs was developed for estimation of urinary prostaglandin levels in rats. Drugs were administered orally to rats (Wistar, male, 200-250 g), and water (2.5 ml/100 g body weight) was given 1 hr after drug administration to yield a constant volume of urine. Urine was collected for 4 hr after drug administration, and urinary PGE2 and PGF2 alpha were determined by radioimmunoassay. The urine volume in the 4-hr period was 5.0 +/- 0.30 ml per rat, and prostaglandin contents in the 4-hr urine were 4.56 +/- 0.56 ng PGE2 and 1.31 +/- 0.24 ng PGF2 alpha per rat in the no-drug control group. Administration of nonsteroidal anti-inflammatory drugs decreased the urinary PGE2 and PGF2 alpha dose dependently. The activities of ten typical nonsteroidal anti-inflammatory drugs in reducing urinary PGE2 excretion were compared with their anti-inflammatory activities in rats. A close correlation (r = 0.98, P less than 0.001) between the dose required for 50% reduction of urinary PGE2 excretion and the dose required for 50% inhibition of carrageenin edema was found for each drug. These drugs were also tested for their inhibitory effects on PGE2 biosynthesis in a cultured system of mouse 3T6 fibroblast cells and on prostaglandin synthesizing system in bovine seminal vesicle microsomes. No close correlation was observed between anti-inflammatory activities and inhibition of prostaglandin biosynthesis in vitro.

Animals↗
PubMed1981

Two simple methods for the evaluation of topically active anti-inflammatory steroidal ointments.

Simple laboratory methods for quantitating the topical anti-inflammatory activity of steroidal ointments are described. One is of croton oil ear edema in rats and the other is a new method using homologous passive cutaneous anaphylaxis (PCA) in rats. In order to avoid problems such as the animals' licking and/or rubbing the ointment at the applied sites, which might result in oral uptake, each rat was housed individually and fitted with a plastic collar in the croton oil experiment. The sites of ointment application in the PCA experiment were covered with adhesive plaster. Optimal experimental conditions were as follows. In the former method, ointments were applied to the inside surface of the ear 5 min after the irritant treatment and anti-edematous activity was determined after 6 h. In the latter, ointments were applied 3 h before the antigenic challenge to the dorsal area of animals which had been passively sensitized by anti-serum, and inhibition of the increased permeability was determined 45 min after the challenge. These methods were found to be reliable with respect to sensitivity and reproducibility of data. Ointments of halcinonide, betamethasone-17-valerate, hydrocortisone-17-butyrate, fluocinonide, flumethasone-21-pivalate and beclomethasone-17,21-dipropionate were evaluated by these methods.

Administration, Topical↗
PubMed1978

Purification and characterization of an anti-inflammatory factor (AIF) from bovine serum.

An anti-inflammatory factor (AIF) was highly purified from normal bovine serum. The purified AIF was a polysaccharide which was formed from a low molecular substance Pro-AIF by macromolecularization. AIF showed potent inhibitory activities against carrageenin induced edema in rats and PMN-leucocyte chemotaxis. It showed no inhibition in cutaneous reaction with serotonin, bradykinin or a mediator releaser compound 48/80. No inhibition was also observed in thermally induced pain, reversed passive Arthus reaction and adjuvant polyarthritis in rats. With these results, the role of AIF in inflammation was discussed.

Analgesics↗
PubMed1975

Studies on cathepsins of rat liver lysosomes. II. Comparative studies on multiple forms of cathepsin A.

The multiple forms of cathepsin A (AI, AII, and AIII) purified from the lysosome fraction of rat liver by Sephadex G-200 and DEAE-Sephadex chromatographies were studied comparatively. Forms AI, AII and AIII were stable between pH 3.0 and 5.5, and had pH optima for CBZ-Glu-Phe at 5.6, 5.8, and 5.9, respectively. These activities were rapidly lost on heating above 60 degrees. Their isoelectric points were at 4.7, 4.8, and 4.9, and the Michaelis constants for CBZ-Glu-Phe were calculated as 10, 6.6, and 4.2 X 10(-4)M, respectively. Activity was inhibited by Ag+, Au3+, Hg2+, iodine, and p-chloromercuribenzoate (PCMB). Diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), toluenesuffonyl fluoride (TSF), and sodium dodecyl sulfate (SDS) were inhibitory at a concentration of 10(-3)M. Soybean trypsin inhibitor, pepstatin, leupeptins, and antipain were not inhibitory, while chymostatin caused slight inhibition. No distinct difference was observed in the effects of these compounds on the multiple forms of cathepsin A despite differences in the molecular weights of these forms (100,000, 200,000, and 420,000, respectively). In immuno-diffusion analysis, cathepsin AI, AII, and AIII which had been treated with EDTA, dithiothreitol, PCMB, and a high concentration of NaCl, gave the same precipitin patterns as the untreated enzymes, but treatment with 6 M urea caused a slight alteration of the pattern. After SDS-treatment (50 mM or more), the precipitin lines of these multiple forms fused and gave a single, identical line. This suggests that the different forms of the cathepsin A are all composed of subunits which are immunologically identical or closely related, and that the subunits are mainly bound by hydrophobic forces. This conclusion is supported by results obtained by poliacrylamide gel electrophoresis in the presence of SDS.

Animals↗