The method of determining the most common isotope of lead is by determining the average atomic mass. The formula for determining the average atomic mass is:
Substituting the values in the formula:
The most common isotope of lead is:
Lead - 207.22 amu
The atomic symbol of lead is 
. The atomic number of is 82.
So, the the most common isotope of lead can be written as:
and Lead - 207.22 amu.
Answer:
CH₂
Explanation:
From the question given above, the following data were obtained:
Mass of compound = 1 g
Mass of CO₂ = 3.14 g
Mass of H₂O = 1.29 g
Empirical formula =?
Next, we shall determine the mass of Carbon and hydrogen present in the compound. This can be obtained as follow:
For Carbon, C:
Mass of CO₂ = 3.14 g
Molar mass of CO₂ = 12 + (2×16)
= 12 + 32
= 44 g/mol
Molar mass of C = 12 g/mol
Mass of C =?
Mass of C = molar mass of C/ Molar mass of CO₂ × Mass of CO₂
Mass of C = 12/44 × 3.14
Mass of C = 0.86 g
For hydrogen, H:
Mass of C = 0.86 g
Mass of compound = 1 g
Mass of H =?
Mass of H = (Mass of compound) – (mass of C)
Mass of H = 1 – 0.86
Mass of H = 0.14 g
Finally, we shall determine the empirical formula of the cyclopropane. This can be obtained as follow:
Mass of C = 0.86 g
Mass of H = 0.14 g
Divide by their molar mass
C = 0.86 / 12 = 0.07
H = 0.14 / 1 = 0.14
Divide by the smallest
C = 0.07 / 0.07 = 1
H = 0.14 / 0.07 = 2
Thus, the empirical formula of cyclopropane is CH₂
Ground is used for agriculture, sink water, hose water, and even drinking water (from the aqueducts).
The answer to this question is D.
The production of manganese peroxidase (MnP) by Irpex lacteus, purified to electrophoretic homogeneity by acetone precipitation, HiPrep Q and HiPrep Sephacryl S-200 chromatography, was shown to correlate with the decolorization of textile industry wastewater. The MnP was purified 11.0-fold, with an overall yield of 24.3%. The molecular mass of the native enzyme, as determined by gel filtration chromatography, was about 53 kDa. The enzyme was shown to have a molecular mass of 53.2 and 38.3 kDa on SDS-PAGE and MALDI-TOF mass spectrometry, respectively, and an isoelectric point of about 3.7. The enzyme was optimally active at pH 6.0 and between 30 and 40 degrees C. The enzyme efficiently catalyzed the decolorization of various artificial dyes and oxidized Mn (II) to Mn (III) in the presence of H(2)O(2). The absorption spectrum of the enzyme exhibited maxima at 407, 500, and 640 nm. The amino acid sequence of the three tryptic peptides was analyzed by ESI Q-TOF MS/MS spectrometry, and showed low similarity to those of the extracellular peroxidases of other white-rot basidiomycetes.
