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Biochemistry Practicals

Monday, May 4, 2009. PRACTICAL 8: INTRODUCTION TO ENZYME INHIBITION. Using the same enzyme and substrate from last week, trypsin and BAPNA, the effects of an inhibitor on the rate of the reaction were investigated. The rate of the reaction was measured again as absorbance per minute using a spectrophotometer, the concentration of substrate was increased in the different solutions. The following table of results was obtained:. The graph obtained is the following:. The case would be completely different in...

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Monday, May 4, 2009. PRACTICAL 8: INTRODUCTION TO ENZYME INHIBITION. Using the same enzyme and substrate from last week, trypsin and BAPNA, the effects of an inhibitor on the rate of the reaction were investigated. The rate of the reaction was measured again as absorbance per minute using a spectrophotometer, the concentration of substrate was increased in the different solutions. The following table of results was obtained:. The graph obtained is the following:. The case would be completely different in...
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Biochemistry Practicals | biochemistrypracticals.blogspot.com Reviews

https://biochemistrypracticals.blogspot.com

Monday, May 4, 2009. PRACTICAL 8: INTRODUCTION TO ENZYME INHIBITION. Using the same enzyme and substrate from last week, trypsin and BAPNA, the effects of an inhibitor on the rate of the reaction were investigated. The rate of the reaction was measured again as absorbance per minute using a spectrophotometer, the concentration of substrate was increased in the different solutions. The following table of results was obtained:. The graph obtained is the following:. The case would be completely different in...

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Biochemistry Practicals: PRACTICAL 8: INTRODUCTION TO ENZYME INHIBITION

http://biochemistrypracticals.blogspot.com/2009/05/practical-8-introduction-to-enzyme.html

Monday, May 4, 2009. PRACTICAL 8: INTRODUCTION TO ENZYME INHIBITION. Using the same enzyme and substrate from last week, trypsin and BAPNA, the effects of an inhibitor on the rate of the reaction were investigated. The rate of the reaction was measured again as absorbance per minute using a spectrophotometer, the concentration of substrate was increased in the different solutions. The following table of results was obtained:. The graph obtained is the following:. The case would be completely different in...

2

Biochemistry Practicals: PRACTICAL 4: SEPARATION OF LIPIDS VIA THIN LAYER CHROMATOGRAPHY.

http://biochemistrypracticals.blogspot.com/2009/03/practical-4-separation-of-lipids-via.html

Sunday, March 29, 2009. PRACTICAL 4: SEPARATION OF LIPIDS VIA THIN LAYER CHROMATOGRAPHY. In this practical the lipids present in egg yolk were separated through absorption chromatography using a TLC plate. The concept is similar to paper chromatography, a plate containing a thin hydrophilic layer called a matrix is used, and a non polar solvent is allowed to move up the plate through capillary action. Thus more polar lipids will move more slowly than non polar lipids. April 30, 2009 at 5:12 PM. PRACTICAL...

3

Biochemistry Practicals: May 2009

http://biochemistrypracticals.blogspot.com/2009_05_01_archive.html

Monday, May 4, 2009. PRACTICAL 8: INTRODUCTION TO ENZYME INHIBITION. Using the same enzyme and substrate from last week, trypsin and BAPNA, the effects of an inhibitor on the rate of the reaction were investigated. The rate of the reaction was measured again as absorbance per minute using a spectrophotometer, the concentration of substrate was increased in the different solutions. The following table of results was obtained:. The graph obtained is the following:. The case would be completely different in...

4

Biochemistry Practicals: PRACTICAL 7:THE KINETIC BEHAVIOUR OF ENZYMES

http://biochemistrypracticals.blogspot.com/2009/05/practical-7the-kinetic-behaviour-of.html

Friday, May 1, 2009. PRACTICAL 7:THE KINETIC BEHAVIOUR OF ENZYMES. In this practical it was studied the effect of changing the amount of enzyme and substrate in an enzyme catalysed reaction. The enzyme used was trypsin, and BAPNA, which is an artificial substrate molecule, was used as the substrate. The following table of results was obtained when the concentration of BAPNA was increased:. The following table was obtained when the concentration of enzyme was increased:. May 25, 2009 at 9:06 AM. Extensive...

5

Biochemistry Practicals: PRACTICAL 5 AND 6: PURIFICATION OF BIOMOLECULES

http://biochemistrypracticals.blogspot.com/2009/05/practical-5-and-6-purification-of.html

Monday, May 4, 2009. PRACTICAL 5 AND 6: PURIFICATION OF BIOMOLECULES. The minus symbol represents no colour, whereas the symbol represents intensity being the maximum intensity. In the case of protein the colour developed was blue whereas in glucose it was red. If a plot of the concentration of the concentration of trypsin and glucose was to be made it would look like the graph below, indicating the separation of the two components. May 25, 2009 at 9:07 AM. Subscribe to: Post Comments (Atom).

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Biochemistry Practicals

Monday, May 4, 2009. PRACTICAL 8: INTRODUCTION TO ENZYME INHIBITION. Using the same enzyme and substrate from last week, trypsin and BAPNA, the effects of an inhibitor on the rate of the reaction were investigated. The rate of the reaction was measured again as absorbance per minute using a spectrophotometer, the concentration of substrate was increased in the different solutions. The following table of results was obtained:. The graph obtained is the following:. The case would be completely different in...

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