What do you think of amino acid sequences for hemoglobin in plants with blank?

a. plants do not contain fat

b. plants contain a different form of hemoglobin then what is found in animals

c. plants do not have blood

d. animals contain a different form of hemoglobin then the type of hemoglobin found in plants

Food webs - transferring energy and matter from one level to another. here you see four food webs. one or more are incorrect. which food web(s) show the correct sequence of organisms, from start to top level consumer? a) a b) d c) c d) a and d

Clara wrote the following hypothesis for an experiment about acidophilic bacteria. bacteria cells will stop dividing in a basic (alkaline) environment because of the high ph. which statement is the best way to restate the hypothesis so that it is more specific? growing acidophilic bacteria in some environments will cause the cells to stop dividing because of ph. if the ph of their environment is changed, acidophilic bacterial cell division will be affected. if the environment of acidophilic bacterial cells becomes alkaline, the bacteria will stop dividing. the more alkaline an environment, the less cell division will occur in bacteria.

Penicillin is hydrolyzed and thereby rendered inactive by penicillinase (also known as β-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(μm) 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.