Search PubMed⌕ Search

Biomedical subjects

F Tanaka

Publications and source records attributed to F Tanaka.

At least 307 records · Page 17Linked to original sources

Interaction of steroids with D-amino acid oxidase.

1. Progesterone inhibited D-amino acid oxidase (D-amino acid : O2 oxidoreductase (deaminating), EC 1.4.3.3) in competition with its substrate, D-alanine. Binding of progesterone brought about the increase in both fluorescence intensity and fluorescence polarization of FAD, which indicates that the environment surrounding FAD chromophore is modified due to a conformational change in the apoenzyme. 2. Ethinyl estradiol, testosterone, testosterone propionate, corticosterone and aldosterone also inhibited the enzyme slightly in the same manner. Their binding also produced a slight increase in FAD fluorescence without decreasing the fluorescence polarization. 3. Cholesterol did not inhibit the enzyme, though it increased the fluorescence polarization of FAD. This indicates the binding of cholesterol with the enzyme at a site other than the substrate binding site.

Animals↗

Changes of serum anti-thyroid antibodies during and after pregnancy in autoimmune thyroid diseases.

Changes of serum anti-thyroglobulin haemagglutination antibodies (TGHA) and anti-thyroid microsomal haemagglutination antibodies (MCHA) were observed during pregnancy and after delivery in Graves' disease and autoimmune thyroiditis. Both TGHA and MCHA decreased as pregnancy progressed, and sometimes they became negative in late pregnancy. Transient increases of TGHA and MCHA were observed after delivery and the antibody titres reached peaks about 3-4 months post-partum in more than halft the patients. In some patients, antibodies developed after delivery. Similar transient increases of antibodies were observed after spontaneous and therapeutic abortion. These changes seem to be induced by physiological and immunological changes occurring during pregnancy and after delivery.

Abortion, Spontaneous↗

Changes of serum immunoglobulins IgG, IgA, IgM, and IgE during pregnancy.

The serum levels of immunoglobulins at various times throughout pregnancy were measured in 11 healthy women. The concentrations of IgG, IgA, and IgM decreased significantly in the second and third trimesters, the mean decreases at the second trimester being 18, 13, and 9%, respectively. When the decreases were expressed on the basis of serum total protein, the decreases in IgG and IgA were significant but the decrease in IgM was not. The level of IgE either decreased or increased during pregnancy. Maternal age, emesis, ABO-incompatibility, and the sex and weight of the baby at birth were not related to the initial concentration or to the extent of decrease of immunoglobulins during pregnancy. In a case of Rh incompatibility, increase of immunoglobulins was observed concomitantly with the transient appearance of anti-Rh(D) antibody. Immunoglobulin depletion in pregnancy seems to result from both immune suppression and hemodilution.

Adult↗

Effect of hydrophobic probes on the higher structure of D-amino acid oxidase.

1. The holoenzyme of D-amino acid oxidase [D-amino acid: O2 oxidoreductase (deaminating), EC 1.4.3.3] was found to combine with 1-anilinonaphthalene-8-sulfonate without liberation of its coenzyme, FAD. No energy transfer interaction was found to occur between the bound dye and FAD of the holoenzyme. On the other hand, when the apoenzyme was bound to the dye and then to FAD, energy transfer interaction between the bound dye and bound FAD was observed. In both cases, the dye competes with the substrate, D-alanine. It is concluded that the dye bound to the holoenzyme is oriented in such a special manner that the mutual orientation factor between the dye and FAD becomes very small in magnitude. 2. When the apoenzyme combined with the dye, the monomer-dimer equilibrium of the apoenzyme shifted towards the dimer. On the other hand, 4-monobenzoylamido-4'-aminostilbene-2,2'-disulfonate combined with the apoenzyme to induce monomerization.

Alanine↗

Effect of alcohols on the structure and function of D-amino-acid oxidase.

The absorption spectrum of D-amino-acid oxidase (D-amino-acid:oxygen oxidoreductase (deaminating), EC 1.4.3.3) was significantly perturbed by various alcohols; typical fine structures were observed in the visible absorption bands, accompanied by blue shifts of the peaks. Both fluorescence intensity and fluorescence polarization were increased upon the addition of alcohols, indicating that the coenzyme is not liberated from the apoenzyme but the hydrophobicity of the environment of the enzyme-bound flavin is increased. Upon the addition of alcohols, the circular dichroism of the enzyme was markedly modified in the visible and near-ultraviolet regions, while that of the apoenzyme in the near- and far-ultraviolet regions was scarcely modified, indicating a change in the interaction between the flavin coenzyme and protein. Both the apparent maximal velocity and the apparent Michaelis constant of the enzyme were increased by the addition of alcohols. The presence of alcohols tends to dissociate the dimer of this enzyme into the monomer, but the dissociation does not fully explain the increase in the maximal velocity of the enzyme by alcohols, because the increase in the maximal velocity caused by alcohols is larger than that expected from the dissociation. Since the rate of formation of the purple intermediate was decreased by alcohols in both the dimer and the monomer, the increase in the maximal velocity could be ascribed to an increase in the rate of dissociation of the enzyme-product complex. This increase could be ascribed to the protein conformational change, which is probably provoked by combination of alcohols with the enzyme at a locus other than that for substrate binding.

1-Propanol↗

Transient recurrence of hyperthyroidism after delivery in Graves' disease.

Four patients with Graves' disease whose hyperthyroidism was in remission following antithyroid therapy were studied without any treatment during and after pregnancy. In the 8-9th month of pregnancy, they were in a euthyroid state with serum levels of thyroxine (T4) of 18.9, 11.9, 11.2 and 14.5 mug/100 ml, triiodothyronine (T3) of 273, 190, 162 and 244 ng/100 ml and T3 resin sponge uptake (RT3U) of 22, 14, 19 and 16% respectively (normal pregnant range: T4, 7.0-15.0, T3 140-250, RT3U 15-25). At 1-3 months after delivery, hyperthyroidism recurred, as manifested by T4 levels of 17.2, 14.5, 16.7 and 21.7 mug/100 ml, T3 levels of 320, 225, 390 and 464 ng/100 ml and RT3U levels of 34, 34, 43, and 41% respectively (normal non-pregnant range: T4 5.0-12.0, T3 90-190, RT3U 24-37). The recurrence of hyperthyroidism was also demonstrated by serial measurements of serum free T4 and free T3. The thyroid function of all four patients returned spontaneously to the normal range at 4-6 months after delivery. One patient developed hypothyroidism for a short period before regaining the euthyroid state. The titers of serum anti-thyroid microsomal antibodies and levels of serum immunoglobulins decreased during pregnancy and increased transitorily at the time of hyperthyroidism after delivery. Similarly, increases in the levels of thyroid hormones, anti-thyroid antibodies and immunoglobulins were observed transitorily following spontaneous abortion after 4 months' pregnancy in one case. We suggest that the transient recurrence of hyperthyroidism in Graves' disease may be induced by immunological changes after delivery.

Adult↗

Labelling of sarcoplasmic reticulum membranes with 1-dimethylaminonaphthalene-5-sulfonyl chloride.

1. Sarcoplasmic reticulum membranes were labelled with 1-dimethylaminonaphtalene-5-sulfonyl chloride (DnsCl). Analyses of the dansylated membranes demonstrated that the most of the dye was associated with ATPase (ATP phosphohydrolase, EC 3.6.1.3) and phosphatidylethanolamine in the membranes. 2. Dansylation of the membranes could be performed without significant decrease in the ATPase activity. 3. Partial differentiation of fluorescence of Dns-phosphatidylethanolamine from that of Dns-ATPase could be achieved by changing excitation wavelength; Dns-ATPase emmitted in the shorter wavelength region, while Dns-phosphatidylethanolamine emmitted in the longer wavelength region. 4. Fluorescence polarization of the dye bound to the membranes indicated that both the ATPase and phosphatidylethanolamine were strongly immobilized in the membranes, while the ratio of freely rotating dye to the "frozen" dye bound to the ATPase was larger than that bound to the phosphatide.

Adenosine Triphosphatases↗

Abnormal serum lactate dehydrogenase isoenzyme in a case of laryngeal carcinoma and thyrotoxicosis.

An abnormal lactate dehydrogenase (LDH) isoenzyme was found in the serum of a patient with laryngeal carcinoma and hyperthyroidism. On electrophoresis it migrated as an additional band between LDH-1 and LDH-2. Follow-up studies suggested that this higher molecular weight, rather thermostable LDH isoenzyme, might have originated from the cancer tissue, though a possible relationship with the thyrotoxic state cannot be excluded.

Drug Stability↗

The circular dichroism of lysozyme.

The circular dichroism spectra of hen egg white lysozyme, and of lysozyme derivatives in which tryptophan residues 62 or 108, or both, are selectively oxidized, have been measured as a function of pH over the range of 200 to 310 nm. Neither Trp-62 nor Trp-108 is principally responsible for the positive rotational strength in the 280 to 300 nm region. The spectrum in the 200 to 230 nm region is nearly the same in the native protein and in the derivatives, and is little affected by binding of saccharide. These results are used to reinterpret the circular dichroism spectra of the lysozymes and alpha-lactalbumins.

Amino Acid Sequence↗