Help me on these two! iām in 6th grade D:
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Biology, 22.06.2019 15:00
The scales shown in the introduction measure mass, or the amount of matter in a particular object. the scientific law of conservation of mass states that matter cannot be created or destroyed during a chemical reaction, but it can change from one form to another. did the simulation support this scientific law? explain why or why not.
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Biology, 22.06.2019 19:00
Penicillin is hydrolyzed and thereby rendered inactive by penicillinase (also known as Ī²-lactamase), an enzyme present in some resistant bacteria. the mass of this enzyme in staphylococcus aureus is 29.6 kd. the amount of penicillin hydrolyzed in 1 minute in a 10-ml solution containing 10-9 g of purified penicillinase was measured as a function of the concentration of penicillin. assume that the concentration of penicillin does not change appreciably during the assay. penicillin(Ī¼m) amount hydrolyzed(nmol) 1 0.11 3 0.25 5 0.34 10 0.45 30 0.58 50 0.61 (a) plot v0 versus [s] and 1/v0 versus 1/[s] for these data. does penicillinase appear to obey michaelis-menten kinetics? if so, what is the value of km? (b) what is the value of vmax? (c) what is the turnover number of penicillinase under these experimental conditions? assume one active site per enzyme molecule.
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Biology, 22.06.2019 19:30
How do high-energy electrons from glycolysis and the krebs cycle contribute to the formation of atp from adp in the electron transport chain? a. high-energy electrons interact with pyruvic acid to create a phosphate bond with adp, forming atp. b. high-energy electrons supply the needed energy to synthesize atp from the lower-energy adp in the electron transport chain. c. high-energy electrons supply a negative charge which causes the citric acid to oxidize, forming a phosphate group to bond with adp. d. high-energy electrons increase the temperature of adp so it easily reacts to form atp.
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Biology, 22.06.2019 21:30
This is a membrane-bound, disk-shaped compartment inside chloroplasts and cyanobacteria. they are the site of the light-dependent reactions of photosynthesis.
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