Proteinase K, solution
... Proteinase K (CAS: 39450-01-6) is a non-specific serine protease having a very high specific activity (cleaves the carboxylic ends of aromatic, hydrophobic and aliphatic amino acids). It has been used for isolation of mRNA, high molecular weight DNA and to inactivate other enzymatic activities. Prot ...
... Proteinase K (CAS: 39450-01-6) is a non-specific serine protease having a very high specific activity (cleaves the carboxylic ends of aromatic, hydrophobic and aliphatic amino acids). It has been used for isolation of mRNA, high molecular weight DNA and to inactivate other enzymatic activities. Prot ...
- thevignanam
... Glucose is metabolized to pyruvate by the pathway of glycolysis Aerobic tissues metabolize pyruvate to acetyl-CoA, which can enter the citric acid cycle for complete oxidation to CO2 and H2O, linked to the formation of ATP in the process of oxidative phosphorylation ...
... Glucose is metabolized to pyruvate by the pathway of glycolysis Aerobic tissues metabolize pyruvate to acetyl-CoA, which can enter the citric acid cycle for complete oxidation to CO2 and H2O, linked to the formation of ATP in the process of oxidative phosphorylation ...
I. CHEMICAL BASIS OF LIFE, cont
... interactions between 2 or more polypeptide chains folded together. Examples include hemoglobin, collagen, chlorophyll ...
... interactions between 2 or more polypeptide chains folded together. Examples include hemoglobin, collagen, chlorophyll ...
lo_ppt20
... Starch is the carbohydrate storage reservoir in plants Cellulose is the major woody structural component of plants Glycogen is the main carbohydrate storage reservoir in animals Hydrolysis breaks poly and disaccharides into monosaccharides by adding water to break the molecules down – Under acidic o ...
... Starch is the carbohydrate storage reservoir in plants Cellulose is the major woody structural component of plants Glycogen is the main carbohydrate storage reservoir in animals Hydrolysis breaks poly and disaccharides into monosaccharides by adding water to break the molecules down – Under acidic o ...
Electron-Transport Chain and ATP production
... Electron-Transport Chain and ATP production Occurs in the inner mitochondrial membrane where NADH and FADH2 are oxidized back to NAD+ and FAD. They transfer their e- in a series of steps and ultimately to O2: O2 + 4e- + 4H+ → 2H2O The energy released in these e- transfers is used to pump H+ (protons ...
... Electron-Transport Chain and ATP production Occurs in the inner mitochondrial membrane where NADH and FADH2 are oxidized back to NAD+ and FAD. They transfer their e- in a series of steps and ultimately to O2: O2 + 4e- + 4H+ → 2H2O The energy released in these e- transfers is used to pump H+ (protons ...
Lecture_5_Control_of_glycolysis
... The kinase that synthesizes fructose 2, 6-bisphosphate and the phosphatase that hydrolyzes this molecule are located on the same polypeptide chain. Such an arrangement is called a bifunctional enzyme. Phosphorylation of the bifunctional enzyme activates the phosphatase activity and inhibits the kina ...
... The kinase that synthesizes fructose 2, 6-bisphosphate and the phosphatase that hydrolyzes this molecule are located on the same polypeptide chain. Such an arrangement is called a bifunctional enzyme. Phosphorylation of the bifunctional enzyme activates the phosphatase activity and inhibits the kina ...
Vmax Regulation through Domain and Subunit Changes. The Active
... productive catalytic cycle (8). In the context of the PGDH tetramer, a similar change in domain-domain orientation was proposed to be related to the serine control mechanism of PGDH (9). The polypeptide segments necessary for domain reorientation have been identified by both structural and biochemic ...
... productive catalytic cycle (8). In the context of the PGDH tetramer, a similar change in domain-domain orientation was proposed to be related to the serine control mechanism of PGDH (9). The polypeptide segments necessary for domain reorientation have been identified by both structural and biochemic ...
BioH_Cellular Respiration
... embedded in the inner membrane called ATP Synthases. As protons rush back into the matrix via ATP synthases, the potential energy is converted into the kinetic energy of the ATP synthase, which begins to rotate in the membrane. This rotational energy is used to assemble ATP from ADP & P. ...
... embedded in the inner membrane called ATP Synthases. As protons rush back into the matrix via ATP synthases, the potential energy is converted into the kinetic energy of the ATP synthase, which begins to rotate in the membrane. This rotational energy is used to assemble ATP from ADP & P. ...
biochemistry national board exam review
... A. C would be a competitive inhibitor of the enzyme. B. C would be a noncompetitive inhibitor of the enzyme. C. The velocity vs. [S] plot for the enzyme would be the same with or without C. D. With C present, the enzyme would convert substrate to product faster. E. With C present, it would take less ...
... A. C would be a competitive inhibitor of the enzyme. B. C would be a noncompetitive inhibitor of the enzyme. C. The velocity vs. [S] plot for the enzyme would be the same with or without C. D. With C present, the enzyme would convert substrate to product faster. E. With C present, it would take less ...
Slides PPT
... This protein complex binding puts a 90o kink in the DNA and interacts with the alpha subunit of RNA polymerase. Without the cAMP:CAP the lac promoter is a weak promoter varying significantly from the consensus sequence at -10 and -35. The combination of the two controls means beta gal and lac permea ...
... This protein complex binding puts a 90o kink in the DNA and interacts with the alpha subunit of RNA polymerase. Without the cAMP:CAP the lac promoter is a weak promoter varying significantly from the consensus sequence at -10 and -35. The combination of the two controls means beta gal and lac permea ...
BIOCHEMISTRY NATIONAL BOARD EXAM REVIEW
... A. C would be a competitive inhibitor of the enzyme. B. C would be a noncompetitive inhibitor of the enzyme. C. The velocity vs. [S] plot for the enzyme would be the same with or without C. D. With C present, the enzyme would convert substrate to product faster. E. With C present, it would take less ...
... A. C would be a competitive inhibitor of the enzyme. B. C would be a noncompetitive inhibitor of the enzyme. C. The velocity vs. [S] plot for the enzyme would be the same with or without C. D. With C present, the enzyme would convert substrate to product faster. E. With C present, it would take less ...
Transcription Regulation Background: Lactose Background: How
... • This is exerted by a protein known as the Catabolite Activator Protein (CAP) • This protein binds to a site on the DNA within the promoter region and increases the rate of RNA polymerase binding; hence transcription initiation. • It only does this when complexed to cAMP. ...
... • This is exerted by a protein known as the Catabolite Activator Protein (CAP) • This protein binds to a site on the DNA within the promoter region and increases the rate of RNA polymerase binding; hence transcription initiation. • It only does this when complexed to cAMP. ...
Chapter 8
... • The reactant that an enzyme acts on is called the enzyme’s substrate • The enzyme binds to its substrate, forming an enzyme-substrate complex • The active site is the region on the enzyme where the substrate binds ...
... • The reactant that an enzyme acts on is called the enzyme’s substrate • The enzyme binds to its substrate, forming an enzyme-substrate complex • The active site is the region on the enzyme where the substrate binds ...
purification and properties of glutamate dehydrogenase from the
... purified 500-fold to a final specific activity of 37.5/~mol NADH utilized/min mg- 1 protein. The enzyme is a hexamer of tool. wt 350,000 _+ 30,000 and subunit size 57,000 _+ 5000. Both nicotinamide coenzymes were utilized with activity ratios, NADH/NADPH, of 3.5 at pH 6.75 and 11 at pH 7.5; NAD/NADP ...
... purified 500-fold to a final specific activity of 37.5/~mol NADH utilized/min mg- 1 protein. The enzyme is a hexamer of tool. wt 350,000 _+ 30,000 and subunit size 57,000 _+ 5000. Both nicotinamide coenzymes were utilized with activity ratios, NADH/NADPH, of 3.5 at pH 6.75 and 11 at pH 7.5; NAD/NADP ...
Slayt 1 - Prof.Dr.Orhan CANBOLAT
... to the corresponding nucleotides IMP and GMP. • Inability to utilize PRPP in the salvage pathway leads to PRPP accumulation, which, in conjunction with low levels of IMP and GMP, causes chronic allosteric activation of PRPP glutamyl amidotransferase and excessive purine synthesis. • The excess purin ...
... to the corresponding nucleotides IMP and GMP. • Inability to utilize PRPP in the salvage pathway leads to PRPP accumulation, which, in conjunction with low levels of IMP and GMP, causes chronic allosteric activation of PRPP glutamyl amidotransferase and excessive purine synthesis. • The excess purin ...
Structure and function of radical SAM enzymes
... the amino nitrogen and one carboxylate oxygen of the methionine moiety of SAM. The methyl carbon and the closest methyl proton of SAM were estimated to be about 4–5 Å and 3 Å, respectively, from the nearest iron atom [55]. In the derived model, the methionine moiety of SAM forms a five-membered-r ...
... the amino nitrogen and one carboxylate oxygen of the methionine moiety of SAM. The methyl carbon and the closest methyl proton of SAM were estimated to be about 4–5 Å and 3 Å, respectively, from the nearest iron atom [55]. In the derived model, the methionine moiety of SAM forms a five-membered-r ...
Sample Chapters - Pearson Canada
... It may appear from Figure 12.2 that some pathways operate simply as the reversal of other pathways. For example, fatty acids are synthesized from acetyl-CoA, but they are also converted to acetyl-CoA by b-oxidation. Similarly, glucose-6-phosphate is synthesized from pyruvate in gluconeogenesis, whic ...
... It may appear from Figure 12.2 that some pathways operate simply as the reversal of other pathways. For example, fatty acids are synthesized from acetyl-CoA, but they are also converted to acetyl-CoA by b-oxidation. Similarly, glucose-6-phosphate is synthesized from pyruvate in gluconeogenesis, whic ...
... Choice B: The version of Phosphofructose kinase (PFK) in the muscle is different than that from the liver. Although both catalyze the same reaction, they are regulated differently. Based on your knowledge of PFK in the liver, and your knowledge of liver and muscle function, suggest how PFK in the mu ...
Inhibition by D-Glutamate of Growth and Glutamate
... brought to 5 ml. L-Glutamic acid (L-glu) and/or ~ - g l uwere added in suitable amounts to the medium before sterilization ; sucrose and L-glutamine were sterilized separately (the last by filtration) and added aseptically to the sterile medium. Strains. Most of the work was done with strain no. I f ...
... brought to 5 ml. L-Glutamic acid (L-glu) and/or ~ - g l uwere added in suitable amounts to the medium before sterilization ; sucrose and L-glutamine were sterilized separately (the last by filtration) and added aseptically to the sterile medium. Strains. Most of the work was done with strain no. I f ...
HH-Unit-1-PPQs - Dalkeith High School
... b. Describe what happens to the genes of a cell as differentiation occurs. (1) c. i) Explain what happens to cell Y, which leads to the formation of a tumour. ...
... b. Describe what happens to the genes of a cell as differentiation occurs. (1) c. i) Explain what happens to cell Y, which leads to the formation of a tumour. ...
Enzyme
Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions. The molecules at the beginning of the process are called substrates and the enzyme converts these into different molecules, called products. Almost all metabolic processes in the cell need enzymes in order to occur at rates fast enough to sustain life. The set of enzymes made in a cell determines which metabolic pathways occur in that cell. The study of enzymes is called enzymology.Enzymes are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Enzymes' specificity comes from their unique three-dimensional structures.Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal temperature and pH.Some enzymes are used commercially, for example, in the synthesis of antibiotics. Some household products use enzymes to speed up chemical reactions: enzymes in biological washing powders break down protein, starch or fat stains on clothes, and enzymes in meat tenderizer break down proteins into smaller molecules, making the meat easier to chew.