Yeah hannah is right the answer is c
Answer: The simplest way is to determine if a strain is mutant is observing morphology, growth rate, double time, etc but it is accurate if you can prove if the strain is deficient in one aminoacid or can't metabolize lactose, etc.
Explanation: A wildtype strain functions normally, for example, can metabolize as a carbon source, glucose, lactose and other sugars, can synthesize all the aminoacids requered for protein synthesis, etc. If a strain suffers a mutation and it is inheritable, the strain become a mutant. Since several mutations can be silent ones, only those that interfere with a process, can be assesed easyly.
For example, if you have several strains and put them in a lactose medium, but some of them cannot growth means that are lactose mutants. Those strains could carry a mutation in genes that encode lactose degrading enzymes or in regulatory genes of the lac operon, etc.
RrTt ....means brown leaves and tall stems !
so answer is D !
Answer:
six
Explanation:
Professor of Chemistry, University of Minnesota, Minneapolis. Oxygen group element, also called chalcogen, any of the six chemical elements making up Group 16 (VIa) of the periodic classification—namely, oxygen (O), sulfur (S), selenium (Se), tellurium (Te), polonium (Po), and livermorium (Lv).
Answer:
The correct answer is option c. "The apparent value of KM increases with a competitive inhibitor, while it remains unchanged with a noncompetitive inhibitor".
Explanation:
The KM value in an enzymatic reaction is defined as the substrate concentration at which the half of the enzyme molecules are binding with the substrate. A way to distinguish between a competitive and noncompetitive inhibition is that the apparent value of KM increases with a competitive inhibitor, while it remains unchanged with a noncompetitive inhibitor. A competitive inhibitor would make that a higher concentration of substrate is needed, while a noncompetitive inhibitor does not change KM since the inhibitor binds to a site of the enzyme different from the active site.
