Relevant bibliographies by topics / Isoenzyme molecular weight

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Academic literature on the topic 'Isoenzyme molecular weight'

Author: Grafiati
Published: 4 June 2021
Last updated: 16 February 2022

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Journal articles on the topic "Isoenzyme molecular weight"

1

WELLER, DAVID L. "ACIDIC PEROXIDASES OF APPLE ROOTSTOCKS." Canadian Journal of Plant Science 67, no. 1 (January 1, 1987): 293–97. http://dx.doi.org/10.4141/cjps87-042.

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The peroxidase activity in extracts of shoot bark from Michigan State Apple Clone (MAC) 24 and in extracts of roots of MAC 24, East Mailing Long Ashton (EMLA) 27, and Oregon Apple Rootstock (OAR) 1 were characterized as being primarily acidic by broad range sucrose gradient isoelectric focusing. Gel isoelectric focusing (GIEF) using a narrower conventional or immobilized pH gradient showed that this activity could be separated into about a dozen isoenzymes. The GIEF isoenzyme patterns of MAC 24 shoot bark extract peroxidase and root extract peroxidases of MAC 24, EMLA 27, and OAR 1 differed. Similar values were obtained for the molecular weight of the peroxidase activity of these extracts. The results indicate that the acidic isoenzymes of apple peroxidase are of similar size.Key words: Apple, rootstocks (apple), peroxidase, molecular weight, isoenzymes
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2

Najafi, Mohammad, Abazar Roustazadeh, Ali Asghar Moshtaghie, and Mohsen Ani. "Liver Aspartate Transaminase Isoenzymes as Biomarkers of Chronic Exposure to Chromium(VI)." Archives of Industrial Hygiene and Toxicology 64, no. 4 (December 1, 2013): 547–52. http://dx.doi.org/10.2478/10004-1254-64-2013-2358.

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Abstract Exposure to hexavalent chromium compounds is associated with the risk of lung cancer, dermatitis, gastrointestinal ulcers, and other tissue damages. The aim of this study was to compare liver isoenzyme and total serum activities of aspartate aminotransferase (AST) as cytotoxic biomarkers of acute and chronic cytotoxicity of CrVI. We investigated the extent of cell damage caused by chromium(VI) in acute (2.5 mg kg-1) daily doses administered over five days and chronic (0.25 mg kg-1 and 0.5 mg kg-1) daily doses administered over 15 to 60 days by measuring total AST in serum and low molecular weight AST (LMW-AST) and high molecular weight AST (HMW-AST) activities in thirty liver fractions. We also evaluated the kinetic properties and electrophoretic mobility of the LMW- and HMW-AST isoenzymes in liver subcellular fractions. Liver LMW-AST and total serum AST activities significantly decreased after 15 days of exposure (P<0.05). With continued treatment, AST activity increased by 15.67 % (P<0.05). Interestingly, changes in serum AST activity were similar to changes in the liver LMW-AST isoenzyme. Our results confirmed that total serum AST activity may serve as a reliable tissue biomarker for long-term exposures to CrVI, but they also suggest that the LMW-AST isoenzyme could be even more sensitive.
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3

Toups, Erin A., and Enmin Zou. "Epidermal collagenase activity and its induction by 20-hydroxyecdysone in the fiddler crab Uca pugilator." Current Zoology 55, no. 1 (February 1, 2009): 75–80. http://dx.doi.org/10.1093/czoolo/55.1.75.

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Abstract The epidermal collagenase activity and its induction by 20- hydroxyecdysone in Uca pugilator were investigated. Zymographic electrophoresis showed four bands of collagenase activity, 16, 19, 22 and 29 kDa in molecular weight, with the former two accounting for 60% and 36%, respectively, of the total collagenase activity. The collagenase activity varies during the molting cycle. Among the molt stages tested, Premolt Stage D0 exhibited the highest epidermal collagenase activity for both the 16 and 19 kDa isoenzymes and, as the molt stage proceeded, the enzymatic activity of these two isoenzymes decreased, with the lowest activity for both found in Premolt Stage D3-4. Injection of 20-hydroxyecdysone significantly induced the activity of the 16 kDa collagenase in the epidermis of Uca pugilator, suggesting that the activity of this isoenzyme is under molting hormone control. Although 20-hydroxyecdysone injection did not result in a statistically significant increase in the activity of the 19 kDa isoenzyme, a tendency of the induction was nonetheless demonstrated. This is the first report on epidermal collagenase activity and its induction by the molting hormone in a crustacean.
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4

Trbojevic, Jovana, Aleksandra Dimitrijevic, Dusan Velickovic, Marija Gavrovic-Jankulovic, and Nenad Milosavic. "Isolation of Candida rugosa lipase isoforms." Chemical Industry 67, no. 5 (2013): 703–6. http://dx.doi.org/10.2298/hemind120828113t.

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Convenient source of lipases for science and industry is yeast Candida rugosa. Crude preparation of Candida rugosa lipase (CRL) consists of several extracellular lipases. Isoenzyme profile depends on the culture or fermentation conditions. All isoforms are coded by lip pseudogene family; they are monomers of 534 amino acids and molecular weight of about 60 kDa. They share the same catalytic mechanism and interfacial mode of activation. Isoenzymes differ in isoelectric points, post-translational modifications, substrate specificity and hydrophobicity. The presence of different lipase isoforms and other substances (i. e. inhibitors) in crude preparation leads to lack of their productivity in biocatalytic reactions. Purification of specific isoform improves its overall performance and stability. This paper provides an overview of different methods for purification of CRL isoenzymes up to date, their advantages and disadvantages.
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5

Bourtzis, K., and V. J. Marmaras. "Integumental phosphatase isoenzymes from white puparia of Ceratitis capitata: isolation and characterization." Biochemistry and Cell Biology 69, no. 10-11 (October 1, 1991): 731–35. http://dx.doi.org/10.1139/o91-110.

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Two specific alkaline phosphatase forms were identified in the integument of wild-type Ceratitis capitata during transition of larvae to pupae. The separation was achieved by DEAE-cellulose chromatography; alkaline phosphatase 1 and alkaline phosphatase 2 were eluted in 0.1 and 0.4 M KC1, respectively. Both isoenzymes have a molecular weight of approximately 180 000. The pH curve reveals two peaks for both alkaline phosphatases: one at 9.4 and the other at 11.0. The two isoenzymes at both pH optima catalyze the hydrolysis of phosphotyrosine and β-glycerophosphate, but not phosphoserine, phosphothreonine, ATP, or AMP. However, at pH 9.4, alkaline phosphatase 1 is more effective than ALPase 2 and exhibits a preference for phosphotyrosine. The divalent cations Mn2+, Mg2+, and Ba2+ activate the enzymes, while Cu2+ and Zn2+ are inhibitors for both isoenzymes. Both isoenzymes are inactivated by EDTA. The effect of amino acids on enzyme activity was also tested. Alkaline phosphatase 1 is inhibited by L-tyrosine, while alkaline phosphatase 2 is unaffected. L-Phenylalanine has no effect on either isoenzyme. Both isoenzymes are inhibited by urea and 2-mercaptoethanol. Simultaneous addition of urea and 2-mercaptoethanol reveals that ALPase 1 is more sensitive to these inhibitors than ALPase 2.Key words: enzyme, Diptera, integument, phosphatase, isoenzymes, phosphotyrosine.
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6

Caselli, Anna, Maria Letizia Taddei, Chiara Bini, Paolo Paoli, Guido Camici, Giampaolo Manao, Paolo Cirri, and Giampietro Ramponi. "Low Molecular Weight Protein Tyrosine Phosphatase and Caveolin-1: Interaction and Isoenzyme-Dependent Regulation†." Biochemistry 46, no. 21 (May 2007): 6383–92. http://dx.doi.org/10.1021/bi0620858.

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7

Mavrides, Charalampos, and Guylaine Nadeau. "Purification and properties of the cytosolic and mitochondrial forms of aspartate aminotransferase and malate dehydrogenase from rat heart." Biochemistry and Cell Biology 65, no. 3 (March 1, 1987): 239–44. http://dx.doi.org/10.1139/o87-031.

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The present work describes the purification from rat heart of the mitochondrial and cytosolic forms of the enzymes of the malate–aspartate shuttle, aspartate aminotransferase (EC 2.6.1.1) and malate dehydrogenase (EC 1.1.1.37), by a single procedure after the preparation of the original crude extract. In 10 purification steps, the four enzymes were obtained electrophoretically pure in yields ranging from 6 to 54% of their respective isoenzyme levels in the crude extract. Apoenzymes were formed from the aminotransferases by reacting them with cysteine sulfinate and dialyzing. Complete reconstitution was obtained after a brief incubation with pyridoxal phosphate. All four enzymes are dimers. The mitochondrial isoenzymes are of slightly lower molecular weight than their respective cytosolic forms. Michaelis constants and maximal velocities were derived by the use of primary and secondary plots. In general, the properties of the enzymes from rat heart are similar to the properties of the enzymes from other animal sources.
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8

Krejčová, Romana, Květoslava Horská, Ivan Votruba, and Antonín Holý. "Phosphorylation of Purine (Phosphonomethoxy)alkyl Derivatives by Mitochondrial AMP Kinase (AK2 Type) from L1210 Cells." Collection of Czechoslovak Chemical Communications 65, no. 10 (2000): 1653–68. http://dx.doi.org/10.1135/cccc20001653.

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Substrate activity of purine (phosphonomethoxy)alkyl derivatives towards mitochondrial AMP kinase (AK2 type) from L1210 cells was studied. The native AMP kinase, purified nearly to homogeneity, is a monomer with molecular weight 26 kDa. The purified AMP kinase is specific for natural adenine nucleotides (AMP and dAMP) as phosphate acceptors but has a broad specificity to nucleoside 5'-triphosphates as phosphate donors. In addition to adenine acyclic nucleotide analogues, the enzyme is capable of phosphorylating also analogous derivatives containing 2,6-diaminopurine moiety. Kinetic data show that the substrate activity of these acyclic nucleoside phosphonates towards AK2 isoenzyme decreases in the order (S)-HPMPA > (R)-PMPA > PMEA > PMEDAP > (S)-PMPDAP > (R)-PMPDAP >> (S)-PMPA. Acyclic nucleotide analogues do not exhibit any inhibitory activity towards AK2 isoenzyme.
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9

Al-Juraisy1, Amel Taha Yassein, Ameera Aziz Mahmood Al-Juraisy1, Ameera Aziz Mahmood Al-Juraisy1, and Nadia Ahmed Saleh2. "Biochemical and Kinetic Study for the partially purified Lecithin: Cholesterol acyltransferase from serum cardiovascular disease." Tikrit Journal of Pure Science 25, no. 2 (March 17, 2020): 31. http://dx.doi.org/10.25130/j.v25i2.955.

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The study includes partial purification of Lecithin: Cholesterol acyltransferase (LCAT) from the blood serum of a person suffering from atherosclerosis. Several techniques were applied including ammonium sulphate precipitation, dialysis, ion exchange chromatography and electrophoresis. It was found that LCAT has one isoenzyme and the highest activity was (1073.46 × 10-3) unit/ml and a molecular weight of 62 KDa. The study also deals with characterizing of LCAT. It was found that the optimum pH and temp. of the enzyme were 7 and 35ºC. http://dx.doi.org/10.25130/tjps.25.2020.027
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10

Wetsel, WC, WA Khan, I. Merchenthaler, H. Rivera, AE Halpern, HM Phung, A. Negro-Vilar, and YA Hannun. "Tissue and cellular distribution of the extended family of protein kinase C isoenzymes." Journal of Cell Biology 117, no. 1 (April 1, 1992): 121–33. http://dx.doi.org/10.1083/jcb.117.1.121.

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Polyclonal isoenzyme-specific antisera were developed against four calcium-independent protein kinase C (PKC) isoenzymes (delta, epsilon, epsilon', and zeta) as well as the calcium-dependent isoforms (alpha, beta I, beta II, and gamma). These antisera showed high specificities, high titers, and high binding affinities (3-370 nM) for the peptide antigens to which they were raised. Each antiserum detected a species of the predicted molecular weight by Western blot that could be blocked with the immunizing peptide. PKC was sequentially purified from rat brain, and the calcium-dependent forms were finally resolved by hydroxyapatite chromatography. Peak I reacted exclusively with antisera to PKC gamma, peak II with PKC beta I and -beta II, and peak III with PKC alpha. These same fractions, however, were devoid of immunoreactivity for the calcium-independent isoenzymes. The PKC isoenzymes demonstrated a distinctive tissue distribution when evaluated by Western blot and immunocytochemistry. PCK delta was present in brain, heart, spleen, lung, liver, ovary, pancreas, and adrenal tissues. PKC epsilon was present in brain, kidney, and pancreas, whereas PKC epsilon' was present predominantly in brain. PKC zeta was present in most tissues, particularly the lung, brain, and liver. Both PKC delta and PKC zeta showed some heterogeneity of size among the different tissues. PKC alpha was present in all organs and tissues examined. PKC beta I and -beta II were present in greatest amount in brain and spleen. Although the brain contained the most PKC gamma immunoreactivity, some immunostaining was also seen in adrenal tissue. These studies provide the first evidence of selective organ and tissue distributions of the calcium-independent PKC isoenzymes.
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Dissertations / Theses on the topic "Isoenzyme molecular weight"

1

Docherty, Suzanne Margaret. "The molecular isoforms and expression of human alkaline phosphatases, with special reference to the placental isoform." Thesis, Queen Mary, University of London, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.250723.

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