Answer:
Effects of CHD
Explanation:
With less blood flow, your heart doesn't get the oxygen it needs, and that can cause chest pain, called angina, especially when you exercise or do heavy labor It also can affect how well your heart pumps and make the rest of your body short on oxygen, too.
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Full Question:</u>
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Trypsinogen is split by the enzyme enterokinase to form an activated molecule of the protease trypsin. Which of the following would confirm that the activation of trypsin is an example of how a positive feedback mechanism can amplify a biological process?
A. The activated trypsin enzyme can use enterokinase as a substrate
B. The trypsin produced by the reaction is capable of splitting and activating additional trypsinogen molecules
C. If levels of trypsin were to get too high, the trypsin molecules would inhibit the enzyme enterokinase
D. Each mRNA molecule that codes for trypsinogen can be translated repeatedly to form many peptide molecules
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Answer:</u></h3>
Trypsinogen molecules are first split into the active enzyme Trypsin by enterokinase. Then the Trypsin being a protease itself, works on Trypsinogens and converts them to Trypsin. Thus this is a positive feedback.
Option B
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Trypsinogen is a proenzyme which is secreted by pancreas into the duodenum. Enterokinase is a intestinal enzyme that is secreted from the small intestinal glands. Enterokinase works on the Trypsinogens to convert them into trypsin by splitting a peptide chain from the proenzyme. This trypsin then digests a variety of proteins and peptides from diet.
Trypsin is a protease and the proenzyme Trypsinogen is a protein. So trypsin works on the secreted trypsinogens too and amplify the production of trypsin from the trypsinogens to enhance the digestion process. Thus, a positive feedback chain is seen here.
Answer:
Homogeneous mixture
Explanation:
Salt and water have only one face
Answer:
By way of introduction, A260/A280 ratio is use to measure Protein Contamination. This procedure was first described to measure protein purity in the presence of nucleic acids. However it is now commonly used to assess protein contamination of DNA. The method to determine the concentration of protein contamination by using A260/280 ratio method is well explained below by filling in the missing words.
Explanation:
The A260/A280 ratio method estimates protein __purity___ by measuring the absorbance maximum at 280nm caused by the amino acids__cytosine___, ____Adenine____, and ___Guanine_________ Since ___Spectrophotometer____ also absorbs in the UV range, we can correct for this contaminate by measuring the absorbance maximum at ____260nm______ and using the following equation: Concentration (µg/ml) = (A260 reading – A320 reading) × dilution factor × 50µg/ml___ When extrapolated from a standard curve, the Bradford data indicates the amount (in _ug__ ) of __unknown ___ protein found in a sample. If you know the volume of sample that was added to the assay then you can calculate the protein ____concentration ___ of the sample. The coomassie blue dye in the Bradford assay specifically binds primary ¬¬___sulfonic___ and __positive amines__ groups of the amino acid side groups of the proteins. The more the dye binds to the sample, the _anionic_ the blue color will be, and the absorbance at 595¬nm will be_shifted Amax___. A sample with an unusually __protein___ number of ___280nm of Tyrosine __ [give a specific example] amino acids will underestimate the total amount of protein present in the sample.
Answer:
Nucleus
Explanation:
Nucleus controls cells' activities by controlling the synthesis of proteins.
Golgi apparatus involves in the secretion and intracellular transport of a cell.
Ribosome helps the synthesis of proteins only.
Mitochondrion involves in respiration, generating energy for the cell.
