Biochemistry and molecular biology international最新文献

{"title":"Hydrated electron-induced inactivation of tyrosinase in aqueous solution by exposure to cobalt-60 gamma-rays. II. Catecholase activity.","authors":"H. Terato, O. Yamamoto","doi":"10.11501/3119917","DOIUrl":"https://doi.org/10.11501/3119917","url":null,"abstract":"Tyrosinase (0.2 mg/ml) was irradiated with 60Co gamma-rays. The catecholase activity was measured at varying radiation doses under various atmospheric conditions. D0 was found to be 1.25 kGy and hit number to be 2 in N2-saturated solution. OH radical scavengers, t-BuOH and MeOH, had no effect. O2 which is an enhancer of OH-induced enzyme inactivation had little effect. But N2O as a e aq scavenger and Cu++ markedly protected against the inactivation indicating that e aq was the main species to inactivate the enzymatic activity. By Ultrogel chromatography, it was found that the enzymatic activity was lost when this enzyme dissociated into its subunits. Thus, it was concluded that the radiation-induced inactivation was due to the reduction of Cu++ as the active center and the chelater with e aq followed by the dissociation.","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"59 1","pages":"301-7"},"PeriodicalIF":0.0,"publicationDate":"2014-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76260355","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The lysine and methionine rich basic subunit of buckwheat grain legumin: some results of a structural study.","authors":"M K Rout, N K Chrungoo","doi":"10.1080/15216549900202033","DOIUrl":"10.1080/15216549900202033","url":null,"abstract":"<p><p>The 26 kD basic subunit of 280 kD buckwheat grain legumin has been partially characterized by measurement of its fluorescence and CD spectra. The protein has 22% alpha-helix, 36% beta-sheet, 12% beta-turn and 30% random coil secondary structure. In comparison with the basic subunits of other legumin-type proteins, the buckwheat legumin subunit has a high content of lysine and methionine. The protein also has higher ratios of lysine to arginine and methionine to arginine.</p>","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"47 6","pages":"921-6"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/15216549900202033","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21277023","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Porphyria-induced hepatic porphyrinogen carboxy-lyase inhibitor and its interaction with the active site(s) of the enzyme.","authors":"S B de Catabbi,&nbsp;R W de Calmanovici,&nbsp;C Minutolo,&nbsp;C Aldonatti,&nbsp;L C San Martin de Viale","doi":"10.1080/15216549900202063","DOIUrl":"https://doi.org/10.1080/15216549900202063","url":null,"abstract":"<p><p>Porphyrinogen carboxy-lyase is an enzyme that sequentially decarboxylates uroporphyrinogen III (8-COOH) to yield coproporphyrinogen III (4-COOH). In mammals this enzyme activity is impaired by hexachlorobenzene treatment, through generation of an enzyme inhibitor. The interaction of porphyrinogen carboxy-lyase inhibitor, extracted from the liver of hexachlorobenzene-treated rats, with substrate decarboxylation sites on the enzyme, was studied using four different carboxylated substrates belonging to the isomeric III series of naturally-formed porphyrinogens containing 8-,7-,6- and 5-COOH. Similar inhibitor effects were elicited against all the substrates assayed, with the exception of pentacarboxyporphyrinogen III in which decarboxylation was not inhibited to same extent. Enzyme protection assays in the presence of the different substrates, indicated that each porphyrinogen protects its own decarboxylation from inhibitor action. Preincubation of the inhibitor with normal enzyme increased its inhibitory effect. On the other hand, preincubation of both enzyme and inhibitor with superoxide dismutase or mannitol, did not alter inhibitory activity. Preincubation of the inhibitor with a number of amino acids showed that only arginine and its derivative N alpha-Benzoyl-L-Arginine ethyl ester interact with the inhibitor, noticeably reducing its ability to inhibit porphyrinogen carboxy-lyase. Albumin, histidine, serine, cysteine and imidazol, were unable to quench inhibitor activity. The present results indicate that the inhibitor acts at the binding site of each porphyrinogen. Taking into account that arginine is related to enzyme activity, and that histidine is found at the binding site of the substrates, the results suggest that the inhibitor could bind to arginine residues, blocking the access of substrates to histidine and altering the adequate orientation for decarboxylation by masking the positively charged active site necessary for porphyrinogen binding to the enzyme. In addition an indirect effect of the inhibitor mediated through free radicals could be discarded.</p>","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"47 6","pages":"945-56"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/15216549900202063","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21276958","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Total reactive antioxidant potential in human saliva of smokers and non-smokers.","authors":"I Kondakova,&nbsp;E A Lissi,&nbsp;M Pizarro","doi":"10.1080/15216549900202023","DOIUrl":"https://doi.org/10.1080/15216549900202023","url":null,"abstract":"<p><p>Uric acid is the most important non-enzymatic antioxidant present in human saliva. There is a great variability among individuals, both in salivary uric acid content and saliva total reactive antioxidant potential (TRAP). The uric acid present in saliva correlates with plasma uric acid, suggesting that the former is imported from plasma. There are not statistical differences between uric acid or TRAP values in saliva of smokers and non-smokers. Also, smoking a cigarette does not modify the levels of antioxidants present in saliva.</p>","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"47 6","pages":"911-20"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/15216549900202023","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21277022","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Activation of bradykinin B2 receptors increases calcium entry and intracellular mobilization in C9 liver cells.","authors":"J A García-Sáinz,&nbsp;S E Avendaño-Vázquez","doi":"10.1080/15216549900202043","DOIUrl":"https://doi.org/10.1080/15216549900202043","url":null,"abstract":"<p><p>In C9 rat liver cells bradykinin and kallidin increased (approximately 2-fold) the intracellular concentration of calcium, but the B1 agonist, des-Arg9-bradykinin did not. The effect of bradykinin was inhibited by the B2 antagonists, Hoe 140 and N-alpha-adamantaneacetyl-D-Arg-[Hyp3, Thi5,8, D-Phe7]-bradykinin, but not by the B1 antagonist, des-Arg9-[Leu8]-bradykinin. The action of bradykinin was diminished, but not abolished, in medium without calcium. The peptide was able to increase intracellular calcium concentration in cells treated with thapsigargin. Bradykinin action was not observed in cells previously stimulated with this local mediator: however, under the same conditions, angiotensin II induced a clear increase in intracellular calcium concentration. Our data indicate that activation of bradykinin B2 receptors increase intracellular calcium concentrations by inducing both gating of the cation and intracellular mobilization in C9 liver cells. In addition, homologous desensitization was observed.</p>","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"47 6","pages":"927-33"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/15216549900202043","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21277024","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"RAPD profile based genetic characterization of chemotypic variants of Artemisia annua L.","authors":"R S Sangwan,&nbsp;N S Sangwan,&nbsp;D C Jain,&nbsp;S Kumar,&nbsp;S A Ranade","doi":"10.1080/15216549900202053","DOIUrl":"https://doi.org/10.1080/15216549900202053","url":null,"abstract":"<p><p>The annual herbaceous plant, Artemisia annua L., belonging to family Asteraceae, is the natural source of the highly potent antimalarial compound, artemisinin, besides producing valuable essential oil. The plant is at present the sole commercial source for artemisinin production since all the chemical syntheses are non-viable. Therefore, economic and practical considerations dictate that plants with maximum content of artemisinin be found and/or ways to increase their artemisinin content be sought. The key to this selection and breeding is a comprehension of chemical and genetic variability and suitable selection(s) of elites from within the available population. In the present study, RAPD analyses of selected chemotypes from a decade old introduced population in India were carried out using arbitrary primers. The RAPD data clearly indicate the distinction amongst these plants. Further, the detection of highly polymorphic profiles (97 polymorphic markers out of a total of 101 markers) suggests the existence of very high levels of genetic variation in the Indian population despite geographical isolation and opens out a strong possibility of further genetic improvement for superior artemisinin content. UPGMA analyses of RAPD and phytochemical trait data indicate that the wide phytochemical diversity is included within the genetic diversity. These results further support the prospects for selection and breeding of superior artemisinin containing lines.</p>","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"47 6","pages":"935-44"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/15216549900202053","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21276957","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of alpha lipoic acid amide on hexachlorobenzene porphyria.","authors":"G L Vilas,&nbsp;C Aldonatti,&nbsp;L C San Martín de Viale,&nbsp;M C Ríos de Molina","doi":"10.1080/15216549900201903","DOIUrl":"https://doi.org/10.1080/15216549900201903","url":null,"abstract":"<p><p>The aim of this work is to study the effect of thioctamide--the commercial form of alpha lipoic acid amide--on the porphyrinogenic action of hexachlorobenzene (HCB). For this purpose, porphyria was induced in rats by chronic HCB treatment, with or without simultaneous thioctamide administration. Two different groups of rats were used as reference: one treated with vehicle (control) and the other treated with thioctamide (TO). Urine delta aminolevulic acid, porphobilinogen, and porphyrin excretions were lower in the HCB + TO treated group than in the HCB group, and the same happened with liver uroporphyrin accumulation. On the other hand, the second stage of uroporphyrinogen-decarboxylase activity was significantly higher in the HCB + TO group than in the HCB group. delta aminolevulic acid synthase activity was higher in the HCB group. Hepatic thiobarbituric acid reactive substances were lower in HCB + TO group than in HCB group. Thus, we might suggest that TO would decrease HCB effects by means of its free radical scavenging ability, and by having a direct effect on uroporphyrinogen-decarboxylase activity.</p>","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"47 5","pages":"815-23"},"PeriodicalIF":0.0,"publicationDate":"1999-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/15216549900201903","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21234012","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fatty acid profile of Escherichia coli during the heat-shock response.","authors":"R Mejía,&nbsp;M C Gómez-Eichelmann,&nbsp;M S Fernández","doi":"10.1080/15216549900201923","DOIUrl":"https://doi.org/10.1080/15216549900201923","url":null,"abstract":"<p><p>The possible changes in the fatty acid profile of Escharichia coli during heat-shock have been investigated. Bacteria growing in steady-state at 30 degrees C were subjected to an abrupt temperature upshift to 45 degrees C and held at the high temperature for various periods of time in order to elicit the heat-shock response. Fatty acid compositions of lipids extracted from samples taken at different times after the temperature upshift, as well as from cultures in steady-state at 30 and 45 degrees C, were determined by gas-chromatography. It has been found that the total unsaturates to total saturates ratio decreases gradually during heat-shock and that 30 min after the temperature jump, the reduction is equivalent to 57% of the difference between ratios corresponding to steady-state cultures at 30 and 45 degrees C. Consistent with this remodeling of lipid acyl chains, there is a decrease in the excimerization rate of the fluidity probe dipyrenylpropane incorporated into sonicated E. coli lipid extracts. Such modifications occur within the time-span of the heat-shock response, as judged from our previous measurements of the kinetics of change in heat-shock proteins induction ratio. Together, these results indicate that the control of membrane fluidity during the heat-shock response can be accounted for, at least in part, by an important change in the fatty acid composition of Escherichia coli lipids.</p>","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"47 5","pages":"835-44"},"PeriodicalIF":0.0,"publicationDate":"1999-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/15216549900201923","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21234014","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Can serum amyloid A or macrophage colony stimulating factor serve as marker of amyloid formation process?","authors":"R Rysavá,&nbsp;M Merta,&nbsp;V Tesar,&nbsp;M Jirsa,&nbsp;T Zima","doi":"10.1080/15216549900201933","DOIUrl":"https://doi.org/10.1080/15216549900201933","url":null,"abstract":"<p><p>Amyloid formation depends on amyloid precursor production and is influenced by the activity of the underlying disorder and mediated by some proinflammatory cytokines. In this pilot study we tried to find some specific markers that could establish the activity of the disease. We investigated 45 samples of sera and 38 samples of urine from patients (pts) with secondary amyloidosis (AA), primary amyloidosis (AL), systemic autoimmune diseases with renal impairment (Vasc) and healthy controls (Co). Pts with AA had increased plasma levels of TNF alpha (9.97 +/- 4.22 vs. 2.63 +/- 1.34 pg/mL, p < 0.001) and SAA (43.14 +/- 16.0 vs. 3.42 +/- 0.7 ng/mL, p < 0.05) in comparison with Co. Plasma levels of M-CSF in the AA group were significantly increased in comparison with Co (1077.34 +/- 238.6 vs. 137.71 +/- 19.6, pg/mL, p < 0.001) and also in comparison with Vasc (482.24 +/- 86.7 pg/mL, p < 0.05). Urinary excretions of TNF alpha (8.92 +/- 8.1 vs. 0.17 +/- 0.11 microgram/mol creatinine, p < 0.01), sIL-6R (1.39 +/- 1.14 vs. 0.07 +/- 0.05 g/mol creatinine, p < 0.01) and M-CSF (650.2 +/- 153.7 vs. 33.3 +/- 8.6 micrograms/mol creatinine, p < 0.01) in AA were significantly increased in comparison with Co. Pts with AL had increased plasma levels of M-CSF (819.83 +/- 264.2 vs. 137.71 +/- 19.6 pg/mL, p < 0.05) and urinary excretion of M-CSF (865.0 +/- 188.4 vs. 33.3 +/- 8.6 micrograms/mol creatinine, p < 0.01) in comparison with Co. SAA has a low specificity for amyloidosis but is a sensitive acute phase reactant. TNF alpha, a proinflammatory cytokine, may reflect the activity of the underlying diseases in secondary amyloidosis. M-CSF was increased both in plasma and urine in amyloidosis groups and seems to be the most promising (possibly specific) marker of amyloidosis.</p>","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"47 5","pages":"845-50"},"PeriodicalIF":0.0,"publicationDate":"1999-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/15216549900201933","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21234015","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Changes in membrane-bound leucine aminopeptidase activity during maturation and ageing of brain.","authors":"G Arechaga,&nbsp;J M Martínez,&nbsp;I Prieto,&nbsp;M J Ramírez,&nbsp;F Alba,&nbsp;M Ramírez","doi":"10.1080/15216549900201943","DOIUrl":"https://doi.org/10.1080/15216549900201943","url":null,"abstract":"<p><p>Aminopeptidases are believed to be enzymes that regulate the activity of various neuropeptides. However, their physiological role, as well as their mechanisms of regulation, are not well understood. To analyze a part of the regulatory mechanisms that control the activity of these enzymes, the subcellular distribution of membrane-bound leucyl aminopeptidase activity was studied in rat brain during development and ageing. Except in fetuses, the enzymic activity was greatest in the microsomal fraction in all ages tested. Except in microsomal and myelin fractions, compared with fetuses, leucyl aminopeptidase activity showed a decrease in 1-week-old rats and a subsequent increase to adult levels in 1-month-old rats. This profile differed in the microsomal fraction, where the activity increased steadily up to 1-month-old rats. After this age, the activity decreased progressively in 5-month and 24-month-old rats. These results may reflect changes in the functional status of the susceptible substrates during development and ageing.</p>","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"47 5","pages":"851-6"},"PeriodicalIF":0.0,"publicationDate":"1999-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/15216549900201943","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21234016","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}