Biochemistry
Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
Question
Book Icon
Chapter 8, Problem 26P
Interpretation Introduction

Interpretation:

The reason corresponding to the fact that V0 is determined as a fraction of Vmax if the concentration of substrate is equal to 10KM and 20KM is to be stated.

Concept introduction:

A constant which expresses the substrate’s concentration if the velocity of reaction equals to the half of the maximum velocity of the reaction is known as Michaelis-Menten constant. It is denoted by KM.

Blurred answer
Students have asked these similar questions
Choice and Preparation of a Buffer System1. Choosing the proper buffer solution In Protein Precipitation, two liters of 5mM buffer solution with pH 5.2 is needed in the isolation of albumin. Which among the following buffer solution is best fitted for said purpose? Justify your answer.Buffer solutions                                                               pKa  Acetate buffer                                                                  4.73Tris- (hydroxymethy) aminomethane                                 8.08Phosphate buffer                                                               7.20 2. Preparation of the chosen buffer system Calculate and measure the amounts (in grams if solid and in mL if liquid) of weak acid and conjugate base needed to be able to prepare the chosen buffer system in part A above. Express your answer in useful units (that is, prepare it from practical amounts or concentrations of starting materials).
200 ml of a 2% protein solution containing an enzyme that you want to purify. Half of the sample is subjected to method A, consisting of fractionated precipitations and 5 ml of final solution are obtained, with a concentration protein equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml, with protein richness equal to 10 mg / ml and with an activity enzymatic also equal to 2000 U / ml. You want to know: a) Which of the two methods has provided the purest enzyme. b) By which of the methods the greatest amount of enzyme has been obtained.
Quantitative Estimation of Amino Acids by Ninhydrin http://vlab.amrita.edu/?sub=3&brch=63&sim=156&cnt=2 can u help me with question 2 of the assignment questions  Based on the experimental data provided, estimate the amount of amino acid in the given unknown solution by Ninhydrin method. SI No. Volume of standard amino acid solution (ml) Amount of amino acid (µg) OD at 570nm 1 Blank   0 2 0.2   0.12 3 0.4   0.25 4 0.6   0.45 5 0.8   0.55 6 1.0 100 0.68 7 Unknown (0.5ml)   0.41
Knowledge Booster
Background pattern image
Similar questions
SEE MORE QUESTIONS
Recommended textbooks for you
  • Text book image
    Biochemistry
    Biochemistry
    ISBN:9781305577206
    Author:Reginald H. Garrett, Charles M. Grisham
    Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning