Assay of succinate dehydrogenase of after isolation of mitochondria in Cauliflower (Brassica oleracea) using differential centrifugation. Kelly M. Messick‚ Rebecca Conner Department of Biological Sciences‚ Salisbury University‚ Salisbury‚ MD‚ 21801 U.S.A Address for correspondence: Kelly M Messick Department of Biological Sciences Salisbury University Salisbury‚ MD 21801 Phone: 410-546-2060 Fax: 410-543-6433 e-mail: km96536@gulls.salisbury.edu Running title: Assay of succinate dehydrogenase
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stabilizes the inactive T state and blocks the catalytic site which needs to be open for enzyme activity to occur. The glycogen phosphorylase b was purified with hydrophobic column chromatography and the concentration was determined with a Bradford Assay. The kinetics of glycogen phosphorylase b were studied by finding a molar extinction coefficient‚ 0.1617 mM cm-1 A-1‚ for
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exhibited an orange coloration—indicative of a weak positive result. Quantification processes for albumin were determined using Warburg-Christian and Bradford Assays. Both method involved spectrophotometry. The resulting protein concentrations in Warburg-Christian were 1.0042 mg/ml for precipitate 1 and 0.7427 mg/ml for precipitate 2. The Bradford Assay for precipitate 1 (test tubes 7‚ 8 and 9) yielded 7.47‚ 8.97 and 8.28 μg/ml and for precipitate 2 (test tubes 8 and 9) gave 6.44 and 4.73 μg/ml in that
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various assays with differing variables. To do so a baseline assay (undiluted extract and room temperature H2O2) was used within the experiment with only one other variable changed in the other assays. These variables included a boiled‚ frozen and then thawed‚ and frozen potato extract and dH2O instead of the potato extract. It was noted that the temperature and or way the potato extract was prepared effects how the enzyme with the potato will react. Therefore the results of each assay varied
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enzymes involved in the digestion of proteins‚ fats‚ and carbohydrates; to state their site of origin; and to summarize the environmental conditions promoting their optimal functioning. 2. To recognize the variation between different types of enzyme assays. 3. To name the end products of digestion of proteins‚ fats‚ and carbohydrates. 4. To perform the appropriate chemical tests to determine if digestion of a particular food has occurred. 5. To cite the function(s) of bile in the digestive process.
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“Spectrophotometer” http://www.ruf.rice.edu/~bioslabs/methods/protein/spectrophotometer.html 3. “Spectrophotometer” http://www.chm.davidson.edu/vce/spectrophotometry/Spectrophotometry.html 4. “Bradford Assay” http://www.science.smith.edu/departments/Biochem/Biochem_353/Bradford.html 5. “Bradford Assay” http://ww2.chemistry.gatech.edu/~lw26/bCourse_Information/4581/techniques/bradford/bradford.html
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The Rivalries of Arkansas and Alabama’s College Football Team Dona Rudd COM/170 February 14‚ 2012 John Dague The Rivalries of Arkansas and Alabama’s College Football Team Alabama Crimson Tide college football team is a better team than the Arkansas Razorbacks for three main reasons: First‚ the number one team in the South Eastern Conference (SEC) is Alabama Crimson Tide‚ second Alabama beat the number one team LSU‚ and the most important is Alabama won the South Eastern
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Biochem. J. (1995) 305‚ 17-20 (Printed in Great Britain) 17 RESEARCH COMMUNICATION The effect of low temperatures Nicole MORE‚ Roy M. DANIEL* and Helen H. PETACH on enzyme activity Thermophile Research Unit‚ University of Waikato‚ Private Bag 3105‚ Hamilton 2001‚ New Zealand The stability of two enzymes from extreme thermophiles (glutamate dehydrogenase from Thermococcales strain ANI and f‚- enzymes‚ glucosidase from Caldocellum saccharolyticum expressed in Escherichia
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Carbohydrates are important in metabolic processes for everyday physical and chemical actions. The carbohydrate‚ glucose‚ is a key component in generating adenosine triphosphate‚ also known as ATP. In order to analyze unknown glucose levels‚ a DNS assay was performed. By using 2-hydroxy-3‚5-dinitrobenzoic acid to oxidize the aldehyde group on the carbohydrate‚ the reducing end of glucose increases in absorbance of 540 nm. Using a UV spectrophotometer‚ the concentration was calculated by using a
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C. partellus gut protease and protease inhibitor activity assays. C. partellus gut protease activity was estimated using chromogenic substrate BApNA [Manasi A et al.‚ 2005]. It was dissolved in the DMSO and a final concentration was made to 1mM in 1.0ml‚ Glycine-NaOH buffer (pH 9)‚ assays were carried at 38°C for 30min [Manasi A et al.‚ 2005]. The reaction was terminated by adding of acetic acid (30%) of 200µl [8‚ 9‚ Manasi A et al.‚ 2005 ]. Supernatant (0.5ml) was added to 1M NaOH (0.5ml) and the
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