



In an enzyme-catalyzed reaction, the velocity of the reaction increases with increasing substrate concentration until the enzyme becomes saturated. At saturation, all active sites of the enzyme are occupied by substrate molecules, and the reaction reaches its maximum velocity (Vmax). Further increases in substrate concentration do not increase the velocity because there are no free active sites available.
This relationship is described by the Michaelis-Menten equation and is graphically represented by a hyperbolic curve, as shown in option (1).
| List I | List II |
|---|---|
| A. Adenosine | III. Nucleoside |
| B. Adenylic acid | II. Nucleotide |
| C. Adenine | I. Nitrogen base |
| D. Alanine | IV. Amino acid |
Match the LIST I (Enzyme) with LIST II (Catabolic Products)
| LIST-I | LIST-II | ||
|---|---|---|---|
| (Enzyme) | (Catabolic Products) | ||
| A | \(\beta\)-galactosidase | III | Galactose + glucose |
| B | Lecithinase | I | Choline + H$_3$PO$_4$ + fat |
| C | Urease | IV | CO$_2$ + NH$_3$ |
| D | Lipase | II | Glycerol + fatty acids |
A sphere of radius R is cut from a larger solid sphere of radius 2R as shown in the figure. The ratio of the moment of inertia of the smaller sphere to that of the rest part of the sphere about the Y-axis is : 
AB is a part of an electrical circuit (see figure). The potential difference \(V_A - V_B\), at the instant when current \(i = 2\) A and is increasing at a rate of 1 amp/second is:
Three identical heat conducting rods are connected in series as shown in the figure. The rods on the sides have thermal conductivity 2K while that in the middle has thermal conductivity K. The left end of the combination is maintained at temperature 3T and the right end at T. The rods are thermally insulated from outside. In steady state, temperature at the left junction is \(T_1\) and that at the right junction is \(T_2\). The ratio \(T_1 / T_2\) is 