Answer:
in male lion, two methyl groups are present in its structure while in female lion, two hydroxl groups are present in its structure
Explanation:
The chemical structure of the carbon atom is different in both male and female lion because both male and female lions have different sex harmones which are totally different from one another. In male lion, testosterone is a sex hormone whose chemical formula is C19H28O2 and two methyl groups and one hydroxl group are present in its structure while in female lion, oestradiol is a sex hormone having a chemical formula C18H24O2 and two hydroxyl groups are present.
Anti-D immunoglobulins or anti-D (RH) immunoglobulins are a variety of immunoglobulins (IgG). These are proteins that play an important role in our immune system.
Anti-D immunoglobulins are obtained from human blood taken from volunteer donors. They are administered in the pregnant woman in case of incompatibility of rhesus between her and the child.
The CPT codes are:
90384 an 90385 for intramuscular use
.
90386 for intravenous use.
The icd-10-cm code is Z29.13.
Answer:
E. 1/600
Explanation:
Hint:
The probability of fixation of a new neutral mutation is 1/(2N)
Given N as 300
= 1/(2×300)
=1/600
Therefore,
1/600 gives a sure fixation of one allele from the large population
Answer:
a) The response indicates that a pH below or above this range will most likely cause enolase to denature/change its shape and be less efficient or unable to catalyze the reaction.
b)The response indicates that the appropriate negative control is to measure the reaction rate (at the varying substrate concentrations) without any enzyme present.
c)The response indicated that the enolase has a more stable/functional/correct/normal protein structure at the higher temperature of 55°C than at 37°C because the enzyme is from an organism that is adapted to growth at 55°C.
Explanation:
Enolase catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during both glycolysis and gluconeogenesis.In bacteria, enolases are highly conserved enzymes and commonly exist as homodimers.
The temperature optimum for enolase catalysis was 80°C, close to the measured thermal stability of the protein which was determined to be 75°C, while the pH optimum for enzyme activity was 6.5. The specific activities of purified enolase determined at 25 and 80°C were 147 and 300 U mg−1 of protein, respectively. Km values for the 2-phosphoglycerate/phosphoenolpyruvate reaction determined at 25 and 80°C were 0.16 and 0.03 mM, respectively. The Km values for Mg2+ binding at these temperatures were 2.5 and 1.9 mM, respectively.
Enolase-1 from Chloroflexus aurantiacus (EnoCa), a thermophilic green non-sulfur bacterium that grows photosynthetically under anaerobic conditions. The biochemical and structural properties of enolase from C. aurantiacus are consistent with this being thermally adapted.
