'Michaelis menten equation' diaporamas de présentation

Unit 3

Unit 3. Enzymes. Catalysis and enzyme kinetics. OUTLINE. 3.1. Characteristics of biological catalysts. Coenzymes, cofactors, vitamins Enzyme nomenclature and classification 3.2. Enzyme catalysis. Transition state Active site Enzyme-substrate complex

1.02k views • 56 slides

Handout 4

Handout 4. Enzymes. Enzyme. Catalysts for biological reactions Most are proteins Lower the activation energy Increase the rate of reaction up to 10 7 fold Activity lost if denatured May contain cofactors such as metal ions or organic compounds

1.06k views • 48 slides

Chapter 14

Chapter 14. Enzyme Kinetics to accompany Biochemistry, 2/e by Reginald Garrett and Charles Grisham.

802 views • 46 slides

Chapter 14

Chapter 14. Enzyme Kinetics to accompany Biochemistry, 2/e by Reginald Garrett and Charles Grisham.

657 views • 46 slides

Analysis of Protein Purity

Analysis of Protein Purity. Total protein Specific quantification Activity assays Binding assays Detection of impurities HPLC Gel electrophoresis Protein mass spectrometry. Monitoring Progress of Purification Protocol. Total protein (mg) Quantity of protein present in fraction

402 views • 38 slides

Enzymology Lecture 3 and 4 by Rumeza Hanif

Enzymology Lecture 3 and 4 by Rumeza Hanif. Enzyme Kinetics. Enzymes accelerate reactions by lowering the free energy of activation Enzymes do this by binding the transition state of the reaction better than the substrate k1 k2 E+S ? ES ? EP ? E+P

397 views • 36 slides

CLINICAL CHEMISTRY

CLINICAL CHEMISTRY. Enzymes. LECTURE 18. Dr. Shihab A. Al- Baijari. Enzymes.

410 views • 34 slides

Outline

372 views • 20 slides

LAB 3 Enzyme Kinetics

LAB 3 Enzyme Kinetics. Studying ?-galactosidase activity at varying substrate concentrations in the presence and absence of an inhibitor Michaelis-Menten enzyme kinetics Lineweaver Burk plot. Michaelis-Menten Enzyme Kinetics. Steady-state Model: Formation of ES = Disappearance of ES

1.81k views • 16 slides