Can you please complete the table? ( Be specific to the mechanism action of each additives) Number ofStopper ColorAdditive(s)Additive Mechanism of ActionInversions1.2.Red*Glass tubeZero3.4.K3EDTA in liquidEightform5-6.7.8-9.Gray10.11.13.Red/gray andgold14.15.Sodium Heparinand K2EDTAHeparin Inhibits thrombin formation,K2EDTA binds calcium

Blood and biological products are collected and stored in glass tubes for analyzing and…

Answered: Can you please complete the table? ( Be…

Phlebotomy Essentials

6th Edition

ISBN:9781451194524

Author:Ruth McCall, Cathee M. Tankersley MT(ASCP)

Publisher:Ruth McCall, Cathee M. Tankersley MT(ASCP)

Chapter1: Phlebotomy: Past And Present And The Healthcare Setting

Section: Chapter Questions

Problem 1SRQ

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Similar questions

Please help me with finding the hypotheses that are being testing in each of the three enzyme experiments(the three tables below), and predicting the results of each of the three experiments based on the hypotheses (if/then). The laboratory experiment is enzyme activity.
graph the data from the table after taking recipocals of [S], V without inhibitor and V with inhibitor. It should be Lineweaver - Burke. use graph paper or excel. however upload graph and answers as 1 document as jpeg, pdf, or word. there should be 2 lines on 1 graph and both lines should cross the Y axis and hit the X axis (negative X axis). label both axes, determine Km and Vmax (show work) in the presence and absence of inhibitor State type of inhibition and if inhibitor resembles the substrate or not. can more substrate relieve the inhibition? [S] (UM) 3 10 30 5 90 Velocity (umol minute-¹) No inhibitor 10.4 14.5 22.5 33.8 40.5 Inhibitor 4.1 6.4 11.3 22.6 33.8
A biochemist wants to determine the effect of an inhibitor on a certain enzyme. The data are shown below: Vo (mM/min) (without inhibitor) Vo (mM/min) (with inhibitor) [Substrate] (mM) 15 1.11 0.67 30 1.81 1.17 45 2.28 1.56 60 2.62 1.88 90 3.09 2.36 Using linear regression analysis, determine the values of Vmax and Km of the enzyme in the ab- sence of an inhibitor. - y-int = - slope = - vmax = - Km =
Find an enzyme that is used by humans for some industrial or useful process (apart from its original purpose; e.g. food production, textiles, agriculture, clinical diagnosis, medical treatment, biofuel production, material polymerization, etc.). How do we obtain or harvest the enzyme? What reaction(s) does it catalyze, and how is this useful for its industrial purpose? 200 words only
Draw the Michaelis-Menten graph you would predict for the enzyme using 50 nM and 100 nM of enzyme in your assays.
If the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme inhibitor is inhibitor reversible or irreversible? And why?
The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (µM). 1.3 - Inhibitor + Inhibitor 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Vmax of the inhibited enzyme reaction?
You put 50 uL of 0.1 mg of protein into a 1 cm pathlength cuvette containing 3 mL of LDH reaction mixture and measure a slope of 0.125 abs/min in an LDH assay. What is the specific activity of the enzyme sample? Show your work.
Please use the graph below to explain the differences between the 2 enzymes whose activities are plotted (enzyme 1-blue and enzyme 2-red). Using appropriate biochemical terminology, how do these differences affect the activity and function of Enzyme 1 versus Enzyme 2? Reaction velocity (vo) Vmax Vmax 2 0 0 Enzyme 1 Enzyme 2 [Substrate]
Below is a simple set of weights obtained while immersing potato slices in various sugar solutions over 30 minutes.!!! For each solution, calculate the rate of weight change over this 30-minute period. Write your answer in standard notation and use 3 digits past the decimal point - e.g. 0.005, 0.030. (Note that the last zero in an answer is considered to be a digit). Show your work with all the calculations I really need the right answer please 0.0 M sucrose = _______ _____________ g/min 0.4 M sucrose = _______ _____________ g/min 0.6 M sucrose = __________________ g/min 0.8 M sucrose = ____________________ g/min 1.0 M sucrose = ____________________ g/min
Angiotensin Converting Enzyme (ACE) inhibitors cause blood vessels to relax, thereby reducing blood pressure. Although Captopril is part of the group of antihypertensive drugs widely used as ACE inhibitors, new research is constantly being carried out with the aim of selecting compounds that are more kinetically advantageous than Captopril. Therefore, a BioPharma employee selected some prototypes and performed kinetic tests, finding the result shown in the figure below. Based on the statement and the graphic above, mark the incorrect alternative. A) It is a graph for determining kinetic parameters according to Lineweaver-Burk. In that case, the coefficient a B) Comparing the prototypes with the reference drug, Prototype 1 has a higher Vmax value. C) Comparing the prototypes with the reference drug, Prototype 2 has a lower Vmax value. D) Captopril has a Vmax of approximately 0.730 and Km of approximately 0.669. E) The two prototypes have Km values lower than those of Captopril and,…
Is the data that you are collecting in the above table quantitative or qualitative? Explain why. Which treatment had the least amount of browning? Which had the most? Why do you think you obtained these results? Remember that the enzyme polyphenol oxidase is a protein! For each treatment, apply your knowledge of how temperature, pH, and salt concentration affect enzyme activity and explain why you got the results that you did. Include bonds and the levels of protein structure that you explored in Activity A in your answer. How does temperature impact the rate of enzyme activity? If you were to leave the apple in the refrigerator longer, why would it eventually brown? Explain based on what you know about enzyme activity. How does pH and its impact on specific types of bonds explain the results you obtained in your lemon juice treatment? Include bonds and levels of protein structure in your answer. How does salt and its impact on specific types of bonds explain the results you obtained…

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