Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB)最新文献

{"title":"Molecular cloning and sequence analysis of a cDNA encoding ornithine decarboxylase cDNA from chilli (Capsicum annuum).","authors":"Zamri Zainal,&nbsp;Roslinda Sajari,&nbsp;Ismanizan Ismail","doi":"10.1080/1025814021000036151","DOIUrl":"https://doi.org/10.1080/1025814021000036151","url":null,"abstract":"<p><p>Ornithine decarboxylase (ODC) is an enzyme of one of the two pathways of putrescine biosynthesis in plants. The genes encoding ODC have previously been cloned from Datura stramonium and human. Using differential screening, we isolated ODC cDNA clone from a cDNA library of ripening Capsicum annuum fruit. The cDNA clone designated CUKM10 contains an insert of 1523 bp. The longest open reading frame potentially encodes a peptide of 345 amino acids with an estimated molecular mass of 47 kDa and exhibit striking similarity to other ODCs. Expression analysis showed that the capODC hybridised to a single transcript with a size of 1.7 kb. The capODC transcript was first observed in early ripening and increased steadily until it reached fully ripening stage. From the observation it is suggested that capODC is developmentally regulated especially during later stage of ripening.</p>","PeriodicalId":83764,"journal":{"name":"Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB)","volume":"6 6","pages":"415-9"},"PeriodicalIF":0.0,"publicationDate":"2002-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24401678","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":"Analysis of distributions of amino acids in the primary structure of apoptosis regulator Bcl-2 family according to the random mechanism.","authors":"Guang Wu,&nbsp;Shaomin Yan","doi":"10.1080/1025814021000036106","DOIUrl":"https://doi.org/10.1080/1025814021000036106","url":null,"abstract":"<p><p>It is no long a question whether the process of evolution is affected by chance, but is to what extent. The random analysis can throw light on the underlying reasoning for the primary structure of proteins. The study on the Bcl-2 family shows that the rank per amino acid increases 93% in bovine than in chicken and rat, which indicates that the effect of chance has more impact on the evolutionary process of chicken and rat Bcl-2 and less impact on bovine Bcl-2. About one fourth of types of amino acids distribute in the highest probabilistic way in the Bcl-2 family. These phenomena are striking in four BH regions where vast majority of amino acids occur with the probabilistically simplest distribution. Mutations and variants can lead to the increased and/or decreased distribution probabilities of amino acids. Mutations 1, 2 and variant 3 target the rank increased in both affected amino acids. By contrast variants 1 and 2 lead to the rank decreased in both affected amino acids. In mutations 3 and 4, the affected amino acids change their ranks to opposite directions, i.e. the rank is lower in replaced amino acid and higher in replacing one. Using our random approaches as quantitative tools, we can measure, compare and explain the primary structures of proteins.</p>","PeriodicalId":83764,"journal":{"name":"Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB)","volume":"6 6","pages":"407-14"},"PeriodicalIF":0.0,"publicationDate":"2002-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24401677","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":"Biochemical and physicochemical changes in collagen isolated from the gall bladder of gall stone patients.","authors":"A Geetha","doi":"10.1080/1025814021000036160","DOIUrl":"https://doi.org/10.1080/1025814021000036160","url":null,"abstract":"<p><p>Abnormal gall bladder motor function with delayed emptying and stasis are the contributory factors of gall stone formation. Since collagen is the major contractile protein, this study was designed to find out whether the biochemical and physicochemical changes of collagen contribute to the pathogenesis of gall stone formation. Collagen was isolated from the gall bladder of 25 gall stone patients undergoing cholecystectomy and from that of 20 gall stone free subjects. The levels of total, soluble and insoluble collagen were determined. The activity levels of collagenase (3.4.23.3) and protease (3.4.24.11) were assessed. Levels of susceptibility of collagen to denaturing agents 2 M potassium thiocyanate and 8 M urea were estimated. Aldehyde content, shrinkage temperature and tensile strength were also determined in isolated collagen. SDS-PAGE was carried out and alpha, beta fractions were quantified. The total and insoluble collagen contents were significantly high in gall stone patients. The activity levels of collagenase and protease were significantly low. Elevated levels of lipid peroxides, aldehyde content, shrinkage temperature and tensile strength were observed in gall stone patients. There is a significant elevation in the beta fraction and a decrease in alpha/beta ratio. Ultramicroscopic structure of gall bladder revealed derangement of collagen fibres and altered tissue architecture. The results showed that the qualitative and quantitative alterations in collagen also contribute for the defective contractility and stasis of gall bladder in gall stone patients.</p>","PeriodicalId":83764,"journal":{"name":"Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB)","volume":"6 6","pages":"421-5"},"PeriodicalIF":0.0,"publicationDate":"2002-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24401679","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":"Evidence for oxidative stress in the gall bladder mucosa of gall stone patients.","authors":"A Geetha","doi":"10.1080/1025814021000036179","DOIUrl":"https://doi.org/10.1080/1025814021000036179","url":null,"abstract":"<p><strong>Background: </strong>There is considerable evidence indicating that gall stone patients have altered gall bladder functions with respect to secretion and absorption and inflammation in mucus membrane when compared with gall stone free subjects. Increased levels of accelerated generation of reactive oxygen species and toxic degradative products of lipid peroxidation have been reported in the plasma of individuals with gall stones. The purpose of this study is to find out whether oxidative stress in mucosa plays any role in the pathogenesis of gall stone diseases. Levels of lipid peroxides, lipid hydroperoxides (LPH) and conjugated dienes were assessed in gall bladder mucosal scrapings obtained from 30 gall stone patients undergone cholecystectomy. Antioxidant enzymes such as catalase (EC 1.11.1.6), superoxidedismutase (EC 1.15.1.1), glutathione peroxidase (EC 1.11.1.9), glutathione transferase (EC 2.5.1.18) and glutathione reductase (EC 1.6.4.2) were assessed. The activity levels of alkaline phosphatase (EC 3.1.3.1), adenosine triphosphatase and protease (EC 3.4.24.11) were also assessed and data compared with identical data collected from 15 gall stone free subjects and 10 post-mortem cases. Gall stone patients had significantly higher levels of conjugated dienes, LPH and thiobarbituric acid reacting substances in their gall bladder mucosa. Lower levels of glutathione and glutathione related enzymes, catalase and superoxide dismutase were observed in those patients when compared to gall stone free subjects. The activities of functional enzymes in mucosa such as alkaline phosphatase, Na(+)-K+ (EC 3.6.1.3) and Ca2+ (EC 3.6.1.2) adenosine triphosphatase showed significant decreases. Histopathological observation showed lipid accumulation, dilated blood vessels, necrotic and fibrotic changes and inflammation in the gall bladder mucosa of gall stone patients. The data show that gall stone patients have a high level of oxidative stress in the gall bladder mucosa, a finding that may be related to a decreased activity of functional enzymes in mucosal cells. Such a condition might result in an altered gall bladder absorption and secretion of bile components such as mucins and glycoproteins. The resultant increased risk of bile saturation would further contribute to the progress of gall stone formation.</p>","PeriodicalId":83764,"journal":{"name":"Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB)","volume":"6 6","pages":"427-32"},"PeriodicalIF":0.0,"publicationDate":"2002-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24401680","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":"Oxidative stress and tumor markers in cervical cancer patients.","authors":"V Manju,&nbsp;V Balasubramanian,&nbsp;N Nalini","doi":"10.1080/1025814021000036115","DOIUrl":"https://doi.org/10.1080/1025814021000036115","url":null,"abstract":"<p><p>Cervical carcinoma is the second most common cancer worldwide. The extent of free radical induced oxidative stress can be exacerbated by the decreased efficiency of antioxidant defense mechanisms. Low levels of essential antioxidants in the circulation have been found to be associated with an increased risk of cancer. The aim of our study was to assess the extent of oxidative stress, the levels of antioxidants like superoxide dismutase (SOD), catalase (CAT), ceruloplasmin and to evaluate tumor markers such as aspartate transaminase (AST), alanine transaminase (ALT), alkaline phosphatase (ALP) and total sialic acid (TSA) levels in circulation of women with cervical carcinoma and to compare our findings with age matched controls. Low levels of SOD and CAT observed in the circulation of cervical cancer patients may be due to their increased utilization to scavenge lipid peroxides as well as sequestration by tumor cells. Higher levels of TSA, AST, ALT and ALP, in the circulation of cervical cancer patients may be used in the diagnosis and treatment monitoring of patients with cervical carcinoma.</p>","PeriodicalId":83764,"journal":{"name":"Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB)","volume":"6 6","pages":"387-90"},"PeriodicalIF":0.0,"publicationDate":"2002-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24401721","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":"Metformin attenuates blood lipid peroxidation and potentiates antioxidant defense in high fructose-fed rats.","authors":"S Srividhya,&nbsp;M K Ravichandran,&nbsp;C V Anuradha","doi":"10.1080/1025814021000024280","DOIUrl":"https://doi.org/10.1080/1025814021000024280","url":null,"abstract":"<p><p>The implication of oxidative stress in the pathology of insulin resistance has been shown recently. We investigated the effect of an insulin sensitizer, metformin, on the plasma lipid peroxidation and antioxidant defense system in the erythrocytes of high fructose fed rats which form an animal model of insulin resistance. The experimental animals were divided into two batches of 12 animals each. The control batch received the control diet, containing starch; the fructose group was given the high fructose diet. At the end of second week these were subdivided into two groups; one was given metformin (50 mg/kg/day in water) by gastric intubation and other group was left untreated. The rats were continued on the same dietary regimen for the next two weeks. Fructose-fed rats showed hyperglycemia, hyperinsulinemia and hypertriglyceridemia at the end of four weeks. Enhanced plasma lipid peroxidation and inadequate cellular antioxidant defense system were observed in them. Administration of metformin was associated with significant normalization of circulating insulin, glucose and triglyceride concentrations. The abnormal triglyceride distribution in the lipoprotein fractions was also ameliorated by metformin therapy. The imbalance between peroxidation and antioxidant defense system was mitigated when fructose-fed rats were treated with metformin. In the control rats, metformin did not affect the parameters studied. Significant positive correlation was obtained between insulin, triglycerides and glucose concentrations with lipid hydroperoxides suggesting that these metabolic variables could influence the lipid peroxide levels in plasma.</p>","PeriodicalId":83764,"journal":{"name":"Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB)","volume":"6 6","pages":"379-85"},"PeriodicalIF":0.0,"publicationDate":"2002-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24401720","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":"A comparative study on the effect of phenobarbitol and beta-methylcholanthrene on glutathione S-transferases of rat testis.","authors":"K N Devi,&nbsp;B Hemavathi,&nbsp;S Aliya,&nbsp;A Raveendra,&nbsp;K Thyagaraju","doi":"10.1080/1025814021000024299","DOIUrl":"https://doi.org/10.1080/1025814021000024299","url":null,"abstract":"<p><p>Glutathione S-transferases (GSTs; EC, 2.5.1.18) ubiquitously distributed in all life forms, are a family of multigene and multifunctional dimeric proteins, which play a main role in drug detoxication. On purification and on electrophoresis, rat testicular glutathione S-transferases showed that it comprises of four subunits, Yc of alpha class, Yb and Ybeta of mu class and Ydelta of pi class. On chromatofocusing they were resolved into six anionic and four cationic isozymes. The substrate specificity studies and immunoblot analysis of testis proteins revealed that Ydelta of pi class GST was induced predominantly in response to phenobarbitol and Yc of alpha class and Ybeta of mu class were elevated specifically on treatment with methylcholanthrene (MC). These results show that structural variation between the two carcinogens induces different types of GST subunits. Therefore, these subunits may be used as marker proteins for specific chemical toxicity of rat testis.</p>","PeriodicalId":83764,"journal":{"name":"Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB)","volume":"6 6","pages":"373-8"},"PeriodicalIF":0.0,"publicationDate":"2002-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24401719","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":"Lead exposure and heat shock inhibit cell proliferation in human HeLa and K562 cells by inducing expression and activity of the heme-regulated eIF-2alpha kinase.","authors":"Angshuman Sarkar,&nbsp;Samit Chattopadhyay,&nbsp;Ruchika Kaul,&nbsp;Jayanta K Pal","doi":"10.1080/1025814021000036124","DOIUrl":"https://doi.org/10.1080/1025814021000036124","url":null,"abstract":"<p><p>We have used human cell lines, namely, K562 and HeLa cells as model systems in understanding the mechanism of lead toxicity and heat shock, that may be mediated by the heme-regulated eIF-2alpha kinase which is also called the heme-regulated inhibitor (HRI). RT-PCR analysis using HRI-specific primers indicated a two- to three-fold increase in HRI expression in K562 and HeLa cells exposed to lead acetate and heat shock, respectively. Further, in vitro eIF-2alpha kinase assay indicated a two- to three-fold increase in HRI kinase activity during lead toxicity in K562 cells. This increase in HRI expression and its activity was accompanied by a significant decrease in cell proliferation and cell viability. This is therefore, the first report indicating that both heavy metal exposure and heat shock cause inhibition of protein synthesis not by activation of HRI alone but by its over-expression as well as activation. Our data indicate further that lead-induced inhibition of cell proliferation may be caused due to inhibition of protein synthesis resulted due to induced expression and activity of HRI.</p>","PeriodicalId":83764,"journal":{"name":"Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB)","volume":"6 6","pages":"391-6"},"PeriodicalIF":0.0,"publicationDate":"2002-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24401722","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":"Alpha-mannosidase from the seeds of Triticale.","authors":"A Subha Mahadevi,&nbsp;R Vegiraju Suryanarayana,&nbsp;N Siva Kumar","doi":"10.1080/1025814021000036133","DOIUrl":"https://doi.org/10.1080/1025814021000036133","url":null,"abstract":"<p><p>Seeds of Triticale (hybrid of wheat and rye) contain an N-acetylglucosamine specific lectin that was affinity purified in our laboratory (Siva Kumar, N. and Padma, K. (1996) \"Affinity purification of N-acetyl glucosamine specific lectin. Purification and partial characterization of Triticale lectin\". Biochem. Mol. Biol. Int. 38, 1059-1066). Seed extracts also exhibited alpha-mannosidase activity that was isolated by a combination of ion exchange, hydrophobic chromatography and gel filtration. The purified enzyme is a glycoprotein with 7% carbohydrate and exhibited a native molecular mass of 1,95,000 (+/-5000) on Biogel P-200 and dissociated into two major subunits under reducing conditions of molecular masses 58 and 40 kDa, respectively. Both subunits cross-reacted with an antibody to the well-characterized jack bean alpha-mannosidase, suggesting antigenic similarity between the legume and the cereal mannosidases. Purified enzyme binds to Con A-Sepharose gel, possibly through the sugar-binding site. Purified Triticale enzyme was stable at 50 degrees C up to 20 min and did not show requirement of metal ions for activity. Phenylalanine was detected as the sole N-terminal amino acid in the purified enzyme.</p>","PeriodicalId":83764,"journal":{"name":"Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB)","volume":"6 6","pages":"397-400"},"PeriodicalIF":0.0,"publicationDate":"2002-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24401723","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":"2-Methylaminopyridine-copper (II) complex catalyzes protein degradation.","authors":"Omali Y El-Khawaga,&nbsp;Ibrahim H El-Sayed","doi":"10.1080/1025814021000039473","DOIUrl":"https://doi.org/10.1080/1025814021000039473","url":null,"abstract":"<p><p>To investigate the mechanism of scission of proteins by the chemical cleaving agents like metal complexes, bovine serum albumin (BSA) has been treated by the copper(II) complex CuL2SO4, where L is 2-methylaminopyridine. BSA degradation increased with increasing the concentration of the copper complex. Copper complex rapidly degraded BSA at mild acidic and neutral pH values while no degradation occurred at alkaline pH values. Moreover, the degradation was increased at higher temperatures. Copper complex act as a catalyst for the polypeptide hydrolysis. The protein degradation was protected with beta-mercaptoethanol by acting as radical scavenger. H2O2 increased BSA degradation which is apparent by the disappearance of the original band. H2O2 reacts with copper complex to produce a reactive oxygen species (ROS), such as hydroxyl radical or a metal-coordinated oxo or peroxo species, which in turn can initiate cleavage of the peptide backbone nearby.</p>","PeriodicalId":83764,"journal":{"name":"Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB)","volume":"6 6","pages":"433-6"},"PeriodicalIF":0.0,"publicationDate":"2002-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24401681","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}