Table K₁ (T1) Vmax (T1) Kt (T2) Vmax (T2) 1.12 mM 125 nmole/min 3.0 mM 130 nmole/min Based on these values, what are your conclusions? None of the above. O T1 is most likely a cell that expresses a high affinity transporter for glucose. T2 is most likely a cell that expresses a high affinity transporter for glucose. T1 must be a cell expressing the insulin-dependent glucose transporter. Each transporter has a similar Vmax and therefore both T1 and T2 are the same cell type.

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### Table

| Parameter      | Value |
|----------------|-------|
| \( K_t \) (T1) | 1.12 mM |
| \( V_{max} \) (T1) | 125 nmole/min |
| \( K_t \) (T2) | 3.0 mM |
| \( V_{max} \) (T2) | 130 nmole/min |

### Analysis and Conclusion

Based on these values, what are your conclusions?

1. ○ T1 is most likely a cell that expresses a high affinity transporter for glucose.
2. ○ T2 is most likely a cell that expresses a high affinity transporter for glucose.
3. ○ T1 must be a cell expressing the insulin-dependent glucose transporter.
4. ○ Each transporter has a similar Vmax and therefore both T1 and T2 are the same cell type.
5. ○ None of the above. 

### Explanation

The table provides kinetic parameters, \( K_t \) and \( V_{max} \), for two cell types, T1 and T2. \( K_t \) (Michaelis constant) indicates the substrate concentration at which the reaction rate is half of \( V_{max} \). A lower \( K_t \) value suggests a higher affinity of the transporter for glucose. 

- **T1** has a \( K_t \) of 1.12 mM, indicating higher affinity compared to T2.
- **T2** has a \( K_t \) of 3.0 mM, indicating lower affinity for glucose.
- Both T1 and T2 have similar \( V_{max} \) values (125 and 130 nmole/min respectively), suggesting similar maximum rates of glucose transport.

Therefore, the most logical conclusion is that **T1 is a cell that expresses a high affinity transporter for glucose**, given its lower \( K_t \) value.
Transcribed Image Text:### Table | Parameter | Value | |----------------|-------| | \( K_t \) (T1) | 1.12 mM | | \( V_{max} \) (T1) | 125 nmole/min | | \( K_t \) (T2) | 3.0 mM | | \( V_{max} \) (T2) | 130 nmole/min | ### Analysis and Conclusion Based on these values, what are your conclusions? 1. ○ T1 is most likely a cell that expresses a high affinity transporter for glucose. 2. ○ T2 is most likely a cell that expresses a high affinity transporter for glucose. 3. ○ T1 must be a cell expressing the insulin-dependent glucose transporter. 4. ○ Each transporter has a similar Vmax and therefore both T1 and T2 are the same cell type. 5. ○ None of the above. ### Explanation The table provides kinetic parameters, \( K_t \) and \( V_{max} \), for two cell types, T1 and T2. \( K_t \) (Michaelis constant) indicates the substrate concentration at which the reaction rate is half of \( V_{max} \). A lower \( K_t \) value suggests a higher affinity of the transporter for glucose. - **T1** has a \( K_t \) of 1.12 mM, indicating higher affinity compared to T2. - **T2** has a \( K_t \) of 3.0 mM, indicating lower affinity for glucose. - Both T1 and T2 have similar \( V_{max} \) values (125 and 130 nmole/min respectively), suggesting similar maximum rates of glucose transport. Therefore, the most logical conclusion is that **T1 is a cell that expresses a high affinity transporter for glucose**, given its lower \( K_t \) value.
Expert Solution
Introduction

Enzyme kinetics studies the effect of the substrate concentration and other factors on the rate of the reaction. The effect can be plotted as the rate of the reaction versus the independent variable or the cause of the effect. There are different components of the kinetic graph.  Vmax is the highest rate of reaction obtained in the study. It is represented as the mol/hr or min. The Km (Michaelis constant) represents the concentration of the substrate at which the rate of the reaction is half of the Vmax. The units of Km are molar or M. Ka or association constant is measure of binding affinity in terms of free and bound ligand, it does not consider the enzyme-ligand complex. Kd or dissociation constant is inverse of the Ka. 

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