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排序方式: 共有167条查询结果,搜索用时 15 毫秒
1.
Srabani De A. K. Dasmahapatra A. K. Ray A. K. Medda 《Neurochemistry international》1989,14(4):461-465
For elucidation of thyroid hormone-induced responsiveness of fish brain, various doses (0.012, 0.025, 0.05, 0.1, 0.25, 0.5, 1, 2 and 4 μg/g) of triiodothyronine (T3) were injected in Singi fish, Heteropneustes fossilis (Bloch), for 3 consecutive days and the changes in cytosolic NADP-dependent malic enzyme (ME, EC 1.1.1.40) activity in whole brain tissue were determined. Compared to the control, the ME activity increased with lower doses (0.012, 0.025 and 0.05 μg/g) and decreased with higher doses (1, 2 and 4 μg/g) of T3, showing a biphasic nature of thyroid hormone action. The enzyme activity remained unaltered with 0.1, 0.25 and 0.5 μg of T3/g in comparison to the control. Immersion of the fishes in cycloheximide-containing medium (0.5 mg/l) inhibited the T3 (0.025 μg/g)-induced rise in ME activity. On the other hand, the NAD-dependent cytosolic malate dehydrogenase (EC 1.1.1.37) activity and the total protein content of brain cytosol remained unaltered with all doses of T3 used. The thyroid hormone specificity of cytosolic NADP-dependent malic enzyme in fish brain is thus documented. 相似文献
2.
Spermine is a substrate of lentil (Lens culinaris) seedling amine oxidase and the oxidation products are reversible inactivators of the enzyme. The spermine is oxidized at the terminal amino groups to a dialdehyde: 2 moles of hydrogen peroxide and 2 moles of ammonia per mole of spermine are formed. The pH optimum of the enzyme with spermine is 7.9 in TI-HCI buffer; the Km value is 4.4·10−4 molar, similar to that found with other substrates (putrescine and spermidine). 相似文献
3.
Single injections of various doses (0.1, 0.25, 0.5, 5 and 20 micrograms/g) of T3 significantly increased the cytosolic malic enzyme activity (delta OD/min/mg cytosolic protein) in liver of Singi fish Heteropneustes fossilis Bloch, in a dose-dependent nature, maximum up to 5 micrograms/g dose on the 3rd day in comparison to the control. There was no difference in the enzyme activity between 5 and 20 micrograms/g of T3 doses. When the enzyme activity was expressed per mg DNA, the dose-dependent increase in the malic enzyme activity was observed upto 0.5 microgram/g of T3, whereas a fall in the enzyme activity was noticed with 5 and 20 micrograms/g of T3 doses. Lowering the dose of T3 to 0.05 microgram/g was without any effect on the malic enzyme activity (delta OD/min/mg cytosolic protein or DNA). Hepatic cytosolic protein content showed a biphasic nature of variation, significant increase with single injections of 0.05, 0.1, 0.25 and 0.5 microgram/g and a fall with 5 and 20 micrograms/g of T3 doses in comparison to the untreated control. Cycloheximide treatments of the Singi fishes counteracted both the T3-induced rise in the hepatic cytosolic malic enzyme activity (delta OD/min/mg cytosolic protein or DNA) and the hepatic cytosolic protein contents. Thiourea-treated hypothyroid fishes showed significantly decreased level of malic enzyme activity (delta OD/min/mg cytosolic protein or DNA) and cytosolic protein content in liver. A single injection of T3 at 0.25 microgram/g to the thiourea-treated fishes not only recovered but also increased the enzyme activity and cytosolic protein content above the untreated control values.(ABSTRACT TRUNCATED AT 250 WORDS) 相似文献
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Na+K(+)-ATPase activity in the liver and muscle microsomal membranes have been determined by different doses (0.1, 0.25, 0.5, 1 and 2 micrograms/gm of body weight) of L-triiodothyronine and L-thyroxine in the toad, Bufo melanostictus. The minimum effective dose of T3 was 0.5 microgram/g in case of both liver and muscle to stimulate the enzyme activity and there was dose dependent rise between T3 at the doses of 0.5 and 1 microgram/g. T3 at the doses of 1 and 2 micrograms/g produced more or less the same level of activity. T4 showed an increased activity at 1 and 2 micrograms/g without any dose dependent fashion in the two organs. The doses 0.1 and 0.25 microgram/gm body weight of T3 and 0.1, 0.25 and 0.5 microgram/gm body weight of T4 remained ineffective to elicit any response in both organs. The grain showed no significant change in the enzyme activity at any of the applied doses of T3 and T4. Cycloheximide inhibited T3 induced rise in Na+K(+)-ATPase activity of liver and muscle. Treatment with propylthiouracil caused a significant fall in Na+K(+)-ATPase activity of liver and muscle and the normal value was restored in the two organs after three consecutive injections of T4 at the dose of 1 microgram/g. 相似文献
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This minireview deals the enzymatic transformation of some amino acids as arginine and ornithine, amines as tyramine, putrescine, spermine and spermidine, and other substances as nitric oxide and thiocyanate. These reactions, catalyzed by two proteins purified from the latex of Euphorbia characias, a copper/quinone containing amine oxidase and a cationic peroxidase, show enzymatic activity interactions probably occurring between these proteins in Euphorbia latex. 相似文献
9.
A. Padiglia Rosaria Medda Jens Z. Pedersen Alessandro Finazzi Agrò Anita Lorrai Barbara Murgia Giovanni Floris 《Journal of biological inorganic chemistry》1999,4(5):608-613
The reaction with substrates and carbonyl reagents of native lentil Cu-amine oxidase and its modified forms, i.e. Cu-fully-depleted,
Cu-half-reconstituted, Cu-fully-reconstituted, Co-substituted, Ni-substituted and Zn-substituted, has been studied. Upon removal
of only one of the two Cu ions, the enzyme loses 50% of its enzymatic activity. Using several substrates, Co-substituted lentil
amine oxidase is shown to be active but the k
c value is different from that of native or Cu-fully-reconstituted enzyme, while K
m is similar. On the other hand, the Ni- and Zn-substituted forms are catalytically inactive. Enzymatic activity measurements
and optical spectroscopy show that only in the Co-substituted enzyme is the organic cofactor 6-hydroxydopa quinone reactive
and the enzyme catalytically competent, although less efficient. The Co-substituted amine oxidase does not form the semiquinone
radical as an intermediate of the catalytic reaction. While devoid or reduced of catalytic activity, all the enzyme preparations
are still able to oxidise two moles of substrate and to release two moles of aldehyde per mole of dimeric enzyme. The results
obtained show that although Co-substituted amine oxidase is catalytically competent, copper is essential for the catalytic
mechanism.
Received: 5 March 1999 / Accepted: 22 July 1999 相似文献
10.
Padiglia A Medda R Lorrai A Murgia B Pedersen JZ Finazzi Agrò A Floris G 《Journal of enzyme inhibition》1999,15(1):91-100
The effect of guanidinium compounds on the catalytic mechanism of pig kidney and lentil seedling amine oxidases has been investigated by polarographic techniques and spectroscopy. Guanidine does not inhibit the lentil enzyme and is a weak inhibitor for pig kidney amine oxidase (K(i) =1 mM), whereas aminoguanidine is an irreversible inhibitor of both enzymes, with a K(i) value of 10(-6) M. 1,4-Diguanidino butane (arcaine) is a competitive inhibitor for both pig and lentil amine oxidases. Amiloride is a competitive inhibitor for pig enzyme, but upon prolonged incubation with this drug the enzyme gradually loses its activity in an irreversible manner. 相似文献