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In 1962, Rachel Carson wrote about the dangers of the pesticide DDT in her book The Silent Spring.

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Q: Who was the Bioligest who wrote aboutthe dangers of dtt?
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What is the function of dithiothreitol in DNA extraction?

DTT is the reducing agent for thiolated DNA


What is the function of DTT during DNA extraction?

Provides reducing conditions which prevent oxidation of the proteins cystidine residues


Why we use reducing agent in protein extraction?

Reducing agents are used to reduce disulphide bonds (-S-S) present within (intrarmolecular) and between (intermolecular) the molecules. S-S bond is formed between two cysteine amino acid (one of the slphur containing amino acids, the other methionine can not form).Reducing agents such as DTT, 2-mercaptoethanol are thus used in extraction buffer to kill the native protein structure.


What is the difference between Fab and Fab'Antibody fragments?

Short answer: Just a few amino acids... Better answer: Antibodies are Y-shaped glycoproteins. The two arms are the antigen-binding fragments (Fab) while the base is the crystalizable fragment (Fc). Fab and Fc are linked by the hinge region. Fab and Fab' are generated by proteolytic cleavage of whole antibodies. Papain cleaves antibodies in the hinge region N-terminal to the interheavy chain disulfide bonds leaving two Fab and a Fc. Pepsin cleave C-terminal to the first S-S bridge therefore Fab remain bonded as F(ab')2. Mild reduction with DTT for example releases the two Fab'. Ig ---(papain)---> 2x Fab + Fc Ig ---(pepsin)---> F(ab')2 + Fc ; F(ab')2 ---(DTT)---> 2x Fab' The heavy chain of Fab' is just a few amino acids longer at the C-terminal end (including a cysteine) than Fab heavy chain.


What is the purpose of a stain in electrophoresis?

I think the Question should be " What is the use of a dye in electrophoresis?" to be more specific, The normal dyes that are incorporated into the sample loading buffer in case of agarose gel is bromophenol blue and xylene cyanol.These are used to track the movement of the sample, so that we can stop the electrophoresis when the dye front is nearly 80%(can vary depending on the molecular weight of the sample) away from the well. In case of polyacrylamide gel electrophoresis the dye has many functions: gives density to the sample so that it sits properly in the well. SDS binds to the amino acid and makes it anionic, so that the movement of the sample is based on molecular weight, if not the charge of the protein will also influence the movement. it also helps us to track the movement of the sample. DTT or mercaptoethanol helps in the breaking of cysteine bonds.. That's it.. But the question is too broad and can be specific!!!!!!!!!1