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mel-nik [20]
3 years ago
12

What is the independent variable (cause) is this experiment?

Biology
2 answers:
rodikova [14]3 years ago
8 0
Types of plant because that varies with the growth
AVprozaik [17]3 years ago
7 0
Answer: types of plant

Explanation: depends or based on growth or the plant
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Physical and cognitive abnormalities in children that are the result of a pregnant woman's heavy drinking are known as
notsponge [240]
I think it's FAS or Fetal Alcohol Syndrome
7 0
3 years ago
Help right now plzzz HURRY NOOW NOW NOW 2 ATTACHMENTS GIVING A BRAINLIEST ANSWER ALL 4
sergey [27]
21. on first attachment is secondary succession
22. is the degree of variation of life....
genetic, species or ecosystem within a specific area, system or planet

23. the last one is wrong = )
3 0
3 years ago
In experimental tests of enzyme evolution, a gene encoding an enzyme was subjected to multiple cycles of random mutagenesis and
ryzh [129]

Answer:

Using directed evolution, we have selected an adipyl acylase enzyme that can be used for a one-step bioconversion of adipyl-7-aminodesacetoxycephalosporanic acid (adipyl-7-ADCA) to 7-ADCA, an important compound for the synthesis of semisynthetic cephalosporins. The starting point for the directed evolution was the glutaryl acylase from Pseudomonas SY-77. The gene fragment encoding the β-subunit was divided into five overlapping parts that were mutagenized separately using error-prone PCR. Mutants were selected in a leucine-deficient host using adipyl-leucine as the sole leucine source. In total, 24 out of 41 plate-selected mutants were found to have a significantly improved ratio of adipyl-7-ADCAversus glutaryl-7-ACA hydrolysis. Several mutations around the substrate-binding site were isolated, especially in two hot spot positions: residues Phe-375 and Asn-266. Five mutants were further characterized by determination of their Michaelis-Menten parameters. Strikingly, mutant SY-77N266H shows a nearly 10-fold improved catalytic efficiency (k cat/K m) on adipyl-7-ADCA, resulting from a 50% increase in k cat and a 6-fold decrease in K m, without decreasing the catalytic efficiency on glutaryl-7-ACA. In contrast, the improved adipyl/glutaryl activity ratio of mutant SY-77F375L mainly is a consequence of a decreased catalytic efficiency toward glutaryl-7-ACA. These results are discussed in the light of a structural model of SY-77 glutaryl acylase.

Semisynthetic cephalosporins and penicillins are the most widely used antibiotics. All clinically important semisynthetic cephalosporins are made from 7-aminocephalosporanic acid (7-ACA)1 or 7-aminodesacetoxycephalosporanic acid (7-ADCA). 7-ACA is derived from cephalosporin C (aminoadipyl-7-ACA), which is obtained by fermentation of the fungus Cephalosporium acremonium. Deacylation is performed either chemically or by a two-step enzymatic process using aD-amino acid oxidase and a glutaryl acylase. The latter enzyme can be found in several Pseudomonas andAcinetobacter species (1-7) as well as in some Gram-positive bacteria (8, 9). 7-ADCA is produced from penicillin G made by Penicillium chrysogenum involving several polluting chemical steps followed by enzymatic deacylation by penicillin acylase (10). A first step toward the introduction of a simplified, more environmentally friendly production of 7-ADCA was the development of a genetically modified P. chrysogenum that produces adipyl-7-ADCA (AD-7-ADCA) (11). For the deacylation of this novel β-lactam, an adipyl acylase is needed. Since the presently identified acylases show little or no activity toward AD-7-ADCA, it is of interest to investigate whether a glutaryl acylase can be converted into an adipyl acylase.

In the past few years, directed evolution has been successfully implemented in changing the substrate specificity of several enzymes (12, 13), resulting in biocatalysts with novel activities. It has become clear that the success of a directed evolution experiment greatly depends on the availability of a good selective substrate, which unfortunately is absent for most bioconversions (12). Artificial substrates that mimic one of the desired catalytic steps may be used for selection; however, it is not clear to what extent the resulting mutants will have lost activity on their natural substrate.

Here we describe a strategy to evolve the glutaryl acylase ofPseudomonas SY-77 into an adipyl acylase with an improved activity toward AD-7-ADCA. The glutaryl acylase fromPseudomonas SY-77 has proven to be particularly suitable for developing an industrial process for deacylation (14). The natural action of the enzyme seems to be directed at hydrolyzing diamino acids with a glutaryl side chain as judged from its high activity on glutaryl-7-A(D)CA. It appears that the enzyme also has a low activity on AD-7-ADCA but no activity on cephalosporin C (2).

Explanation: I know my stuff I get B's in school.

3 0
4 years ago
How much energy is available at the third trophic if the first trophic Level has aout 300,000 kJ available energy and the loss r
boyakko [2]

3,000 kilijoules.

You go from 300,000 at the first trophic level to 30,000 at the second trophic level, and finally 3,000 at teh third.

5 0
3 years ago
Giardia does it lead to elevated levels of IgE and eosinophilia?
vaieri [72.5K]

Answer:

No, Giardia is a protozoan that does not cause eosinophilia.

Explanation:

Eosinophilia refers to an increase in the number of eosinophils in the blood. The eosinophil is one of the white blood cells. When this occurs, the circulating eosinophils might be over 400 or 500.

Many factors might cause. One of them is parasite infections, in which helminths trigger the IgE generation, producing eosinophilia.

In the presence of the parasite antigen, eosinophils have a shorter medullar generation time, and they express a higher number of receptors for IgE and IgG. Their function is to damage the parasite, directly or indirectly, and to decrease the damages caused by their presence.

Giardia, among other protozoans, does not cause eosinophilia. Yet some other protozoans and parasites might induce it.

4 0
3 years ago
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