Answer:
A. Because they are compounds, they cannot be pure substances.
Explanation:
The false statement from the given choices is that because they are compounds they cannot be pure substances. In fact, because they are compounds they are pure substances.
Pure substances are made up of elements and compounds and they have the following properties:
- All parts are the same throughout
- Composition is definite
- They cannot easily be separated or broken
- Separation by physical method is not easy
- They have unique sets of physical and chemical properties.
Answer:
Isotopes have same atomic numbers, no. of protons and no. of electrons. Only their no. of neutrons and atomic mass are changed.
<u>Na - 24:</u>
Atomic Mass = 24
Atomic No. = 11
Hence,
No. of protons in Na-24 = 11
No. of neutrons = Atomic Mass - Atomic Number
No. of neutrons = 24 - 11
No. of neutrons = 13
Atomic Number = 11
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Hope this helped!
<h3>~AH1807</h3><h3>Peace!</h3>
Answer:
Eurkaryote... sorry if i wrong
Explanation:
Answer:
hope this helps!
Explanation:
In a chemical change, the atoms in the reactants rearrange themselves and bond together differently to form one or more new products with different characteristics than the reactants. When a new substance is formed, the change is called a chemical change
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.
