1. Using the structure of d-TMP show all the structural fragments donated by different organic compounds during d-TMP synthesis (in the structure each fragment must be shown using arrow directed from the donor's name). 2. Reasons for hyperuricemia state in humans and its diagnostics.
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![Variant 2
1. Using the structure of d-TMP show all the
structural fragments donated by different organic
compounds during d-TMP synthesis (in the
structure each fragment must be shown using
arrow directed from the donor's name).
2. Reasons for hyperuricemia state in humans and
its diagnostics.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fa232d2b3-6d5c-4e54-bd1d-7dc092ceaeca%2F07e98467-f988-44ef-8bff-1119dd088f9d%2Fn73gxbq_processed.png&w=3840&q=75)
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- Enzymes MATCHING TYPE a.Erepsin b.Sutilains c.Chymotrypsin d.Urokinase e.Fibrinolysin f.Rennin g.Papain h.Alcalain i.Bromelains j. Pepsin 1.Additive to remove protein stains 2. Relieve symptoms of episiotomy 3. Isolated from human urine or obtained from human kidney cells by tissue culture techniques. 4. Treatment of blood clots within the cardiovascular system, exclusive of thrombi of the coronary and cerebral ateries. 5. Obtained from the stomach of Sus scrofa, Fam. Suidae and has a proenzyme: pepsinogen which is activated by HCl. 6. From Bacillus subtilis, used as wound debridement. 7. Coagulating enzyme that is present in the mucous membrane of the stomach of animals. Important in cheese making. 8. Crystallized from an extract of the pancreatic gland of Ox Bos Taurus used as an ophthalmic solution. 9. Mixture of protein-digesting & milk clotting enzymes from the juice of Ananas comosus used as meat tenderizer. 10. Found in the intestinal juice, Converts proteoses and…6. Serum blood of a patient with dislipoproteinemia type I has milky appearance even in fasting. If serum stays at low temperature (4) for several hours, the fatty layer appears on its surface. What are the possible causes of these symptoms? Answer the questions and do the following tasks: a) what compounds of serum blood must be tested in the patient in a biochemical lab? b) what is the possible diagnosis of the discase? c) draw the reaction which does not occur properly in the patient's blood; d) explain how the products of the previous reaction are used in adiposc tissue and heart in a healthy person I hour after meal.b. Cleavage with chymotrypsin produces the following fragments: Band A: CN , NLQY, GIVEQCCHKRSEY Band B: F, Y, DPTKM, IACCVRGF, RTTGHLCGKDLVNALY Cleavage with Staphilococcus aureus V8 protease produces the following fragments: Band A: GIVE, YNLQNYCN, QCCHKRCSE Band B: PTKM, RTTGHLCGKD, LVNALYIACGVRGFFYD What is the amino acid sequence of the protein? Type your response
- 15 Explain why detergents, which have an amphipathic structure like bile salts, are able to remove both water-based and oil-based stains.9 Give four therapeutic functions that aspirin (acetyl salicylic acid) has. Explain each in details.I. A protein, X, was Isolated from a pathogenlc mlcroorganism. The proteln Is a vlrulence factor whose path0genlclty lies In a heptapeptide of unknown sequence. After trypsin cleavage of the heptapeptide from protein X, the peptlde's compOsition and sequence was determined. The fOllowing were the results of the sequenclng process: 1. When the peptide was treated with dinitrofluorobenzene (DNFB), DNP-asp and a mixture of amino acids were produced. 2. When the same Intact peptide was treated with streptococcal protease, a pentapeptide of composition asp, asN, cys, gly and ser and 2 amlno acids were released. 3. When the heptapeptlde was also treated with hydrOxylamine HCI, a tripeptide and a tetrapeptide were obtained. The C-terminal amino acid of the tripeptide was asN. 1) What is the sequence of the heptapeptide if it is composed of cys, asp, lys, asN, gly and ser only? 2) What is the pl of the heptapeptide?
- 4 A I. Refer to the figure below and answer the following questions: 45 5 55 6 65 PH 7 75 8.5 0 10 B 15 20 25 30 35 Temperature (°C) 40 45 Legend: Blue - wild-type ß-galactosidase; Red - mutant ß-galactosidase a. What is the optimum pH of wild type ß-galactosidase? b. What is the optimum temperature of mutant ß-galactosidase? c. Which enzyme has the greater activity at pH 7.2? d. Which enzyme has the greater activity at a temperature of 42.5°C? e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4? f. Which enzyme has greater activity if temperature increases from 40°C to 41 °C? 50 55Rabbits were in injected with [32 P] photsphate intraperitoneally ans asacrificed after 2, 5, 8, 12, 18, 24, 48, or 168 hours of radioisotope administration. DNA, nuclear RNA (nRNA), and cytoplasmic RNA (cRNA) were prepared from the kidneys and their specific activities (radioactivity/ mg of nucleic acid) were determined 1. what can be concluded from the nRNA and cRNA curves and why 2. why didn thte specific acitivies of nRNA's and cRNA's decrease significantly after 2 days of labeling.PROTEINS 1. What will happen to free arginine after being subjected to biuret analysis (is it positive or negative, include color)2. What will happen to beef extract after being subjected to ninhydrin analysis (is it positive or negative, include color)
- 1. Briefly describe the affect of the glutamic acid to valine mutation on the Hemoglobin protein as it relates to Sickle Cell Anemia. 2. Is your prediction (from question 3 in Part I) consistent with the description of the cause of the sickle-cell anemia disease (from the BME3D computer tutorial)? Explain.2B. S. aureus hemolysin B attacks the RBC cell membrane by hydrolyzing the sphingomyelin headgroup: ОН HN .R hemolysin B cuts this bond i) Draw a plausible mechanism of hydrolysis for this lipid headgroup. Let B- and BH be general base and general acid. 00-P-O LOR2 OR, ii) Why is this damaging to the overall membrane architecture of the RBC?1. suggest a simple procedure (or test) to veify if the final prodeuct you obtained from the extraction of casein in milk is indded casein. 2. what are the three general steps involved in isolation of proteins> discuss briefly and describe the purpose of each step. 3. what is the purpose of ethanol in the isolation of casein from milk.
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