Journal of applied biochemistry最新文献

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Biochemical comparison of myeloperoxidase of leukemic myeloblasts and normal neutrophilic granulocytes. 白血病成髓细胞与正常中性粒细胞髓过氧化物酶的生化比较。
Journal of applied biochemistry Pub Date : 1984-10-01
K Morishita, S Asano, H Fujii, J Yokota, H Kodo, S Miwa
{"title":"Biochemical comparison of myeloperoxidase of leukemic myeloblasts and normal neutrophilic granulocytes.","authors":"K Morishita,&nbsp;S Asano,&nbsp;H Fujii,&nbsp;J Yokota,&nbsp;H Kodo,&nbsp;S Miwa","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Myeloperoxidases were purified from leukemic myeloblasts (Mbl-MPO) and from normal neutrophilic granulocytes (Gra-MPO) and were compared with each other biochemically. Gel filtration studies showed that the molecular weights (Mr) of Mbl-MPO and Gra-MPO were about 70,000 and 130,000, respectively, so that the former is almost one-half the molecular size of the latter. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis with 2-mercaptoethanol, both MPOs split into two major subunits, heavy and light peptide chains. However, each of these chains of Mbl-MPO seemed to be smaller than that of Gra-MPO, Mr 58,000 versus Mr 62,000 for the heavy chain and Mr 12,000 versus Mr 15,000 for the light chain. On the other hand, another band of Mr 34,000 also appeared in Mbl-MPO under nonreducing conditions and in both MPOs after being boiled. The size of this band was not different in the two MPOs, but the ratio of this band to the others was much higher in Mbl-MPO. The activity of Mbl-MPO could be demonstrated in the heavy chain of Mr 58,000, using a blotting method, and was found to be less heat stable than that of Gra-MPO. These findings indicate that Mbl-MPO may represent an incomplete, unstable half-enzyme form of Gra-MPO.</p>","PeriodicalId":14978,"journal":{"name":"Journal of applied biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17167732","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}
引用次数: 0
An enzymatic synthesis of 4-methyl-L-glutamic acid diastereoisomers. 4-甲基- l-谷氨酸非对映异构体的酶法合成
Journal of applied biochemistry Pub Date : 1984-10-01
A Righini-Tapie, R Azerad
{"title":"An enzymatic synthesis of 4-methyl-L-glutamic acid diastereoisomers.","authors":"A Righini-Tapie,&nbsp;R Azerad","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>(2S,4R)-\"erythro\"- and (2S,4S)-\"threo\"-4-methylglutamic acids have been prepared by glutamate dehydrogenase-catalyzed reductive amination of 2-keto-(R,S)-4-methylglutaric acid, in the presence of NH4+ ions, NAD+, and a NADH recycling system (ethanol-alcohol dehydrogenase), followed by separation by anion-exchange chromatography. Nuclear magnetic resonance, electrophoretic, chromatographic, and optical properties of both isomers are reported, together with the conditions leading to the four-carbon epimerization.</p>","PeriodicalId":14978,"journal":{"name":"Journal of applied biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17592896","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}
引用次数: 0
Purification and properties of malolactic enzyme from Lactobacillus murinus CNRZ 313. 鼠乳杆菌cnrz313苹果酸乳酸酶的纯化及性质研究。
Journal of applied biochemistry Pub Date : 1984-10-01
A M Strasser de Saad, A A Pesce de Ruiz Holgado, G Oliver
{"title":"Purification and properties of malolactic enzyme from Lactobacillus murinus CNRZ 313.","authors":"A M Strasser de Saad,&nbsp;A A Pesce de Ruiz Holgado,&nbsp;G Oliver","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The malolactic enzyme of Lactobacillus murinus was purified 79 fold. Mr = 220,000 as determined by gel filtration and gradient gel electrophoresis. The enzyme consists of two apparently identical subunits (Mr = 110,000) that were observed after treatment with sodium dodecyl sulfate. NAD protected the enzyme against inactivation and its addition, after dissociation, restored the malolactic activity. The apparent Km's for malate, NAD, and Mn2+ were 2.31 X 10(-2), 4.5 X 10(-4), and 1.4 X 10(-4) mM, respectively. Maximum enzymatic activity was observed at 37 degrees C and pH 5.5 in 0.2 M phosphate buffer. At pH values substantially different from the optimum, a positive cooperativity between substrate molecules was observed. The activation energy of the reaction was 8000 and 16,200 cal mol-1 for the temperature values more than and less than 30 degrees C, respectively. Malolactic enzyme catalyzes the NAD and manganese-dependent reaction L-malate----L-lactate + CO2. Therefore, this enzyme can be distinguished from the well-known malic enzymes [L-malate: NAD+ oxidoreductase, oxaloacetate decarboxylating (EC 1.1.1.38) or decarboxylating (EC 1.1.1.39)].</p>","PeriodicalId":14978,"journal":{"name":"Journal of applied biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17592900","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}
引用次数: 0
New method for covalent immobilization of proteins to cellulose and cellulose derivatives. 纤维素及其衍生物共价固定蛋白质的新方法。
Journal of applied biochemistry Pub Date : 1984-10-01
M A Krysteva, S R Blagov, T T Sokolov
{"title":"New method for covalent immobilization of proteins to cellulose and cellulose derivatives.","authors":"M A Krysteva,&nbsp;S R Blagov,&nbsp;T T Sokolov","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Cellulose and microcrystalline cellulose are treated consecutively with sodium periodate and urea. The interaction of urea derivatives with formaldehyde results in highly reactive groups, capable of further condensation with the amino acid residues of the proteins. The condensation of chymotrypsin, pepsin, and ovomucoid with such activated matrices has been studied in the pH interval 2 to 10. Differences have been found in the binding properties of basic and acid proteins. Satisfactory values have been obtained concerning the relative enzymatic and inhibitory activity of the immobilized products with respect to high- and low-molecular substrates. Chymotrypsin, immobilized on microcrystalline cellulose matrix, is found to manifest better catalytic properties compared with chymotrypsin immobilized on cellulose matrix. A probable sequence of the stages of chemical activation of the matrices and covalent binding of the proteins to them has been proposed. The main advantages of the proposed method consist of the high reactivity of the binding group in a wide pH range, its suitable length, and its easy synthesis.</p>","PeriodicalId":14978,"journal":{"name":"Journal of applied biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17501568","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}
引用次数: 0
Conjugates of mitomycin C with the immunoglobulin M monomer fragment of a monoclonal anti-MM46 immunoglobulin M antibody with or without serum albumin as intermediary. 丝裂霉素C与单克隆抗mm46免疫球蛋白M抗体的免疫球蛋白M单体片段结合,有或没有血清白蛋白作为中间体。
Journal of applied biochemistry Pub Date : 1984-10-01
N Umemoto, Y Kato, Y Takeda, M Saito, T Hara, M Seto, T Takahashi
{"title":"Conjugates of mitomycin C with the immunoglobulin M monomer fragment of a monoclonal anti-MM46 immunoglobulin M antibody with or without serum albumin as intermediary.","authors":"N Umemoto,&nbsp;Y Kato,&nbsp;Y Takeda,&nbsp;M Saito,&nbsp;T Hara,&nbsp;M Seto,&nbsp;T Takahashi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>In studies on antitumor antibody-drug conjugates as potential antitumor agents with improved tumor specificity, conjugates of mitomycin C (MMC) with the IgMs fragment of a monoclonal IgM antibody to a tumor-associated antigen (MM antigen) on mouse mammary tumor MM46 cell (anti-MM46 IgMs) were prepared by direct and bovine serum albumin (BSA)-mediated indirect conjugation. MMC was linked to the IgMs and BSA by the use of 1a-[4-(N-succinimidoxycarbonyl)butyryl]mitomycin C, which allowed the slow release of MMC. In the indirect conjugation, the thiol group of BSA was first protected as the 2-pyridyldithio group and, after the MMC binding, regenerated with dithiothreitol, and the resulting BSA-MMC was reacted with the IgMs having the maleimide group introduced with N-succinimidyl m-(N-maleimido)benzoate. Anti-MM46 IgMs-MMC was more cytotoxic against the target MM antigen-positive but Thy 1.2 antigen-negative MM46 cells than control anti-Thy 1.2 IgM-MMC. No such selective cytotoxicity was observed between anti-MM46 IgMs-MMC and anti-Thy 1.2 IgMs-MMC against the MM antigen- and Thy 1.2 antigen-negative MM48 cells. Anti-MM46 IgMs-BSA-MMC was more cytotoxic against MM46 cells than was a mixture of unconjugated anti-MM46 IgMs and BSA-MMC.</p>","PeriodicalId":14978,"journal":{"name":"Journal of applied biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17502713","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}
引用次数: 0
Cobalt--from bacteria to borax bead test. 钴——从细菌到硼砂头测试。
Journal of applied biochemistry Pub Date : 1984-10-01
T H Jukes
{"title":"Cobalt--from bacteria to borax bead test.","authors":"T H Jukes","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":14978,"journal":{"name":"Journal of applied biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17592891","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}
引用次数: 0
Bioluminescent assay of lactate dehydrogenase and its isoenzyme-1 activity. 乳酸脱氢酶及其同工酶-1活性的生物荧光测定。
Journal of applied biochemistry Pub Date : 1984-10-01
M S Pråhl, M T Karp, T N Lövgren
{"title":"Bioluminescent assay of lactate dehydrogenase and its isoenzyme-1 activity.","authors":"M S Pråhl,&nbsp;M T Karp,&nbsp;T N Lövgren","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A bioluminescent assay based on the bacterial luciferase reaction has been developed for the determination of total lactate dehydrogenase and heart-specific lactate dehydrogenase isoenzyme-1 activity in serum. The lactate dehydrogenase-catalyzed reaction was measured in both directions, but NADH formation (lactate----pyruvate) is recommended because it allows the use of optimal reaction conditions. Internal calibration with a known amount of NADH accounts for possible interference from samples when both NADH formation and consumption are followed. The bioluminescent method is sensitive, has good precision, and is readily automated. Serum lactate dehydrogenase isoenzyme-1 was immunochemically isolated and the activity was assayed by bioluminescence. A good correlation between the bioluminescent assays and the conventional spectrophotometric procedure used as reference was obtained.</p>","PeriodicalId":14978,"journal":{"name":"Journal of applied biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17592894","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}
引用次数: 0
Metachromatic staining patterns of basic proline-rich proteins from rat and human saliva in sodium dodecyl sulfate-polyacrylamide gels. 十二烷基硫酸钠-聚丙烯酰胺凝胶对大鼠和人唾液富碱性脯氨酸蛋白的异色染色模式。
Journal of applied biochemistry Pub Date : 1984-10-01
M G Humphreys-Beher, D J Wells
{"title":"Metachromatic staining patterns of basic proline-rich proteins from rat and human saliva in sodium dodecyl sulfate-polyacrylamide gels.","authors":"M G Humphreys-Beher,&nbsp;D J Wells","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A series of basic proteins, rich in proline, were isolated from the salivary secretions of humans and rats. These proteins underwent metachromasia after staining with Coomassie brilliant blue R-250 in sodium dodecyl sulfate-polyacrylamide gels. The technique of destaining gels in several changes of 10% acetic acid after a 30-min staining period is a rapid method of general utility for the identification of proline-rich proteins from total cell lysates from other sources besides saliva.</p>","PeriodicalId":14978,"journal":{"name":"Journal of applied biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17153046","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}
引用次数: 0
Evidence for the presence of fatty acid methyl esters in human hepatoma tissue from a patient with hypercholesterolemia. 高胆固醇血症患者肝癌组织中脂肪酸甲酯存在的证据。
Journal of applied biochemistry Pub Date : 1984-10-01
S Yoshida, T Tamura, M Tamura, M Takeshita, H Terao, T Fujioka, T Itoga
{"title":"Evidence for the presence of fatty acid methyl esters in human hepatoma tissue from a patient with hypercholesterolemia.","authors":"S Yoshida,&nbsp;T Tamura,&nbsp;M Tamura,&nbsp;M Takeshita,&nbsp;H Terao,&nbsp;T Fujioka,&nbsp;T Itoga","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The lipid composition of a human hepatoma tissue (liver cell carcinoma) was examined by thin-layer chromatography (TLC), and an unusual lipid spot was found in a large quantity. It was identified as consisting of fatty acid methyl esters by TLC and gas chromatography-mass spectrometry techniques. In the fatty acid methyl ester fraction, oleate (18:1) and palmitate (16:0) were dominant. Furthermore, very unusual fatty acid methyl esters, such as methyl 2-methyl oleate, were detected. These unusual lipids could be detected neither in cirrhotic lesions of the host liver nor in normal control tissues.</p>","PeriodicalId":14978,"journal":{"name":"Journal of applied biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17167635","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}
引用次数: 0
Practicable enzyme immunoassay for neuron-specific enolase in human serum. 人血清中神经元特异性烯醇化酶的实用酶免疫测定。
Journal of applied biochemistry Pub Date : 1984-10-01
S Kimura, H Uchikawa, R Yamamoto, K Kato
{"title":"Practicable enzyme immunoassay for neuron-specific enolase in human serum.","authors":"S Kimura,&nbsp;H Uchikawa,&nbsp;R Yamamoto,&nbsp;K Kato","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A practicable sandwich-type enzyme immunoassay for neuron-specific enolase (NSE) in human serum was established by the use of purified antibodies to bovine neuron-specific gamma gamma-enolase. The assay system consisted of polystyrene balls (6.5 mm in diameter) with immobilized antibody F(ab')2 fragments and the same antibody Fab' fragments labeled with beta-D-galactosidase from Escherichia coli. The assay could be performed within a working day. The assay system had a minimum detectable sensitivity of 50 pg per assay tube or 1 microgram per liter of NSE in human serum. The assay did not cross-react with nonspecific alpha alpha-enolase and muscle-specific beta beta-enolase. Coefficients of variation in within-assay and between-assay of serum NSE were less than 10%. Serum NSE values (n = 79) determined with the present method correlated well with those obtained by the previously developed method (correlation coefficient r = 0.96, y = 0.92x - 0.83). Serum NSE concentrations of healthy subjects were less than 5 micrograms per liter and those in sera of patients with small-cell carcinoma of the lung were enhanced.</p>","PeriodicalId":14978,"journal":{"name":"Journal of applied biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17458074","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}
引用次数: 0
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