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Biomedical subjects

F Egami

Publications and source records attributed to F Egami.

At least 19 recordsLinked to original sources
PubMed1990

[Treatment of a refractory chronic osteomyelitis of the jaw].

Two cases of refractory chronic osteomyelitis of the jaw were presented, the first in a patient with pycnodysostosis, the second that had been receiving radiotherapy. Both cases were primary chronic osteomyelitis with a markedly protracted course of recovery, in spite of the antibiotic and local irrigation therapy. However the lesion was cured by the removal of sequesters and granulation tissues without radical treatment such as a decorticotomy. Radical surgery, decortication, is an effective procedure in the treatment of chronic osteomyelitis of the jaw, but treatment with the surgical procedures which remove only the necrotic bones and granulation tissues followed by antibiotic therapy is also possible.

Adult↗
PubMed1979

Polymers produced by heating an amino acid mixture in sea water enriched with transition elements.

A mixture of eighteen protein amino acids was heated in sea water medium enriched with transition metal ions. Small granules were obtained as precipitates. Both dialyzable polymers and undialyzable polymers were obtained from the supernatant. Dialyzable polymers yielded mainly Glu, Asp, Ser, and Thr on hydrolysis; undialyzable polymers (C, 29.45; H, 3.87; N, 4.87; and ash, 31.5 wt%) yielded Thr, Asp, Glu, Gly, Leu, Ser, Lys, Pro, His, Phe, and a few unidentified ninhydrin positive peaks after acid hydrolysis. Five wt% of the undialyzable polymers con-ist of acid-hydrolyzable protein amino acids.

Amino Acids↗
PubMed1979

Formation of molecules of biological interest from formaldehyde and hydroxylamine in a modified sea medium.

As reported previously, glycine, serine, aspartic acid, and beta-alanine are the predominant amino acids produced from equimolecular formaldehyde and hydroxylamine in a modified sea medium enriched with essential transition metal ions. The time course of formation of the amino acids, and related substances was studied. Among the amino acids, glycine was produced earlier. Urea was produced initially and disappeared rapidly. Formation of cyanide, glycinenitrile, and glycinamide preceded the formation of amino acids. Probable pathways for the formation of amino acids and urea are suggested.

Amino Acids↗
PubMed1977

Deoxyribonuclease A, a novel deoxyribonuclease highly active toward Polydeoxyadenylic acid and polythymidylic acid from Achatina fulica.

Two novel deoxyribonucleases, termed DNases A and A', have been purified from the hepatopancreas of Achatina fulica (agate snail). DNases A and A' were obtained in 3.6 % and 7.7% yields by acetate buffer extraction and successive chromatography on hydroxyapatite, phosphocellulose and poly(A)-Sepharose. The two DNases are highly active toward poly(dA) and at a salt concentration of 0.15 m and pH 5.0 exhibit 10-fold higher hydrolyzing activities toward poly(dA) than toward calf thymus denature DNA. The enzymes also act considerably on poly(dT) at pH 4.0, but do not appreciably digest other synthetic homopolymers such as poly(dC), poly(dG) and poly(A). The limit products obtained by exhaustive digestion of poly(dA) with DNases A and A' are 98% and 99% acid-soluble and consist of oligonucleotides with an average chain length of about 5 nucleotides containing barely detectable dimers and trimers, respectively. These fragments have terminal 5'-hydroxyl and 3'-phosphate groups. The mode of action appears to be endonucleolytic. Both enzymes have the same pH optimum of 5.0 for poly(dA-hydrolyzing activity. Ionic strength is critical for the maximum activity.

Animals↗
PubMed1977

Selective formation of certain amino acids from formaldehyde and hydroxylamine in a modified sea medium enriched with molybdate.

Amino acids produced from formaldehyde and hydroxylamine in modified sea mediums with different concentrations of molybdate were analyzed. The modified sea mediums contained lower concentration of sodium chloride and higher concentrations of transition metal ions (Zn2+, Fe3+, Cu2+, Co2+, Mn2+ each 10(-4)m, and Mo O4(2-)10(-6), 10(-4), or 10(-2)m) than sea water. The concentration of molybdate had apparently no remarkable effect on the total yields of primary amino groups, but a remarkable effect on the nature of amino acids produced. The formation of alanine, aspartic acid, beta-alanine and, in particular, proline was increased, and that of glycine and serine was decreased with the enrichment of molybdate. The results suggest the possibility of a natural selection of prebiotic organic molecules based on the nature of environmental catalysers in the course of chemical evolution.

Amino Acids↗
PubMed1976

Asparagusate dehydrogenases and lipoyl dehydrogenase from asparagus mitochondria. Physical, chemical, and enzymatic properties.

Asparagusate dehydrogenases I and II and lipoyl dehydrogenase have been obtained in homogeneous state from asparagus mitochondria. They are flavin enzymes with 1 mol of FAD/mol of protein. Asparagusate dehydrogenases I and II and lipoyl dehydrogenase have s20,w of 6.22 S, 6.39 S, and 5.91 S, respectively, and molecular weights of 111,000, 110,000, and 95,000 (sedimentation equilibrium) or 112,000, 112,000, and 92,000 (gel filtration). They are slightly acidic proteins with isoelectric points of 6.75, 5.75, and 6.80. Both asparagusate dehydrogenases catalyzed the reaction Asg(SH)2 + NAD+ equilibrium AsgS2 + NADH + H+ and exhibit lipoyl dehydrogenase and diaphorase activities. Lipoyl dehydrogenase is specific for lipoate and has no asparagusate dehydrogenase activity. NADP cannot replace NAD in any case. Optimum pH for substrate reduction of the three enzymes are near 5.9. Asparagusate dehydrogenases I and II have Km values of 21.5 mM and 20.0 mM for asparagusate and 3.0 mM and 3.3 mM for lipoate, respectively. Lipoyl dehydrogenase activity of asparagusate dehydrogenases is enhanced by NAD and surfactants such as lecithin and Tween 80, but asparagusate dehydrogenase activity is not enhanced. Asparagusate dehydrogenases are strongly inhibited by mercuric ion, p-chloromercuribenzoic acid, and N-ethylmaleimide. Amino acid composition of the three enzymes is presented and discussed.

Amino Acids↗
PubMed1976

Sulphogalactolipid sulphohydrolase activity of arylsulphatase purified from a marine gastropod Charonia lampas.

Sulphatide, cerebroside 3-sulphate was hydrolyzed at a considerable rate by arylsulphatase (aryl-sulphate sulphohydrolase, EC 3.1.6.1) purified from a marine gastropod, Charonia lampas. However, it was scarcely hydrolyzed by glycosulphatase (sugar-sulphate sulphohydrolase, EC 3.1.6.3) from the same origin. The same was observed with seminolipid, a sulphoglycerogalactolipid. The enzymatic characteristics of both sulphogalactolipid and sulphohydrolase activities of the arylsulphatase were determined as follows. The enzyme activities are stimulated by the addition of sodium taurodeoxycholate and MnCl2. The pH optimum of sulphatide sulphohydrolase activity was pH 5.0, while seminolipid sulphohydrolase activity had maximum activity at pH 5.5. Both of these pH versus activity curves were broad. The Km value was 6.22-10-5 M for both substrates. However, the V values were sulphatide were lower by a factor of one-third than those with seminolipid. These enzyme activities were inhibited by substrates of the arysulphatase, i.e., p-nitrophenyl sulphate, p-nitrocatechol sulphate, ascorbate 2-sulphate and each other sulphogalactolipid, but not by glucose 6-sulphate. Sulphate and phosphate anions inhibited both of the enzyme activities.

Animals↗
PubMed1976

Effects of polyamines and analogs on staphylococcal nuclease.

The promoting activity of polyamine analogs (IV approximately XV) on staphylococcal nuclease with DNA as the substrate was compared with that of natural polyamines (I APPROXIMATELY III): I. NH2(CH2)3NH(CH2)4NH(CH2)3NH2(spermine); II. NH2(CH2)3NH(CH2)3NH(CH2)3NH2(thermine); III. NH2(CH2)4NH2 (putrescine); IV. CN(CH2)2NH(CH2)4NH(CH2)2CN; V. HOOC(CH2)2NH(CH2)4NH(CH2)2COOH; VI. C2H5OOC(CH2)2NH(CH2)4NH(CH2)2COOC2H5; VII. HO(CH2)3NH(CH2)4HH(CH2)3OH; VIII. CH3COHH(CH2)3NH(CH2)4NH(CH2)3NHCOCH3; IX. C2H5NH(CH2)3NH(CH2)4NH(CH2)3NHC2H5; X. NH2(CH2)3S(CH2)4S(CH2)3NH2; XI. NH2(CH2)3NH(CH2)2O(CH2)2NH(CH2)3NH2; XII. NH2(CH2)3NCH3(CH2)4HCH3(CH2)3NH2; XIII. CN(CH2)2NCH3(CH2)4NCH3(CH2)2CN; XIV. (CH3)2N(CH2)3NCH3(CH2)4NCH3(CH2)3N(CH3)2; XV. NH2(CH2)2O(CH2)2NH2 Replacement of the terminal groups by CN, COOH, COOEt, NHAc, NHEt, or N(CH3)2 remarkably decreased the activity. The compound VII with terminal hydroxyl groups had a lower promoting activity at low concentrations, but revealed higher activity at higher concentrations and, in contrast to spermine, no inhibition at all even at very high concentrations. Replacement of both internal amino groups by sulfur or NCH3 decreased the activity. The introduction of an ether bond into the internal methylene groups (compound XI) highly decreased the activity. Based upon these findings the possible relationship between structure and activity is discussed.

Animals↗
PubMed1976

Two glycosulfatases from the liver of a marine gastropod, Charonia lampas. Partial purification and properties.

Two glycosulfatases [EC 3.1.6.3], I and II, were purified 31.3- and 33.9-fold respectively, from a crude extract of the liver of Charonia lampas. The purification was carried out by the following chromatographic procedures; phosphocellulose, Sephadex G-150, Concanavalin A-Sepharose and isoelectric focussing. The enzyme preparations obtained were practically free from arylsulfatase [EC 3.1.6.1] contamination. Both glycosulfatases are probably glycoproteins differing in their carbohydrate moieties. The molecular weights of glycosulfatase I and II were estimated to be about 112,000 and 79,000 respectively. They had the same optimum pH of 5.5, and the same Km value of 25.0 mM for glucose 6-sulfate.

Glucose↗
PubMed1976

Synthesis of various phosphodiesters and phosphomonoesters with ribonuclease N.

1. 3'-Guanylyl-ethanol, 3'-guanylyl-propanol, and 3'-guanylyl-alpha-glycerol were synthesized by ribonuclease N1 [EC 3.1.4.8] using guanosine 2',3'-cyclic phosphate as a phosphate donor and various alcohols as phosphate acceptors. The yields of these phosphodiesters were 15%, 13.5%, 38.2%, respectively, with respect to phosphate donor under the optimum conditions. No phosphodiester was synthesized when 2-propanol was used as a phosphate acceptor. Thus, primary alcoholic hydroxyl groups may be regarded as the preferred phosphate acceptor. 2. 3'-Guanylyl-glucose and 3'-guanylyl-ribose were synthesized using glucose and ribose as phosphate acceptors. Under the optimum conditions, the yields of guanylyl-glucose amounted to 52.0%, while that of guanylyl-ribose was much lower. The guanylyl-glucose can be regarded as 3'-guanylyl-6-glucopyranose, based on the results of periodate oxidation. 3. Neither hydroxyamino acids (serine and threonine) nor N-acetylserinamide could be phosphorylated under the conditions used for the above phosphorylations. 4. 3'-Guanylyl-glycerol obtained as above was hydrolyzed by snake venon phosphodiesterase to produce glycerol 3-phosphate. The latter consisted of L-glycerol 3-phosphate (ca 17%) and the D-isomer (ca. 83%). Ribonuclease N1 thus catalyzes an asymmetric synthesis.

1-Propanol↗