12:13 PM LEARNER'S PACKET [LEaP] KS3 IV. LEARNING PHASES AND LEARNING ACTIVITIES V. ASSESSMENT (Time Frome: Day 4, 15 mins) (Leaming Activity Sheets for Errichment, Remedation, or Assessment to be given on Vieesis 3 and b) (Modular) Learning Activity 6. On a one whole sheet of paper, identify the following statements, 1. It is a lem for the flesh of callle, sheep, and pigs. Meal comprises of waler, prolein, fal, and various amounls of minerals and vitamins. 2. A cut of meat taken from the breast of catile. 3. It is obtained from the part of the sheep's body between the forequarter and hindquarter. 4. A cut obtained from the back of deer. 5. Taken from the side of the deer's body. 6. A cut of pork that is obtained from the upper part of the pig's front shoulders. 7. It is the meat of the domestic pig that is used for food. 8. This beef cut is obtained from below the rib or at the front belly of the cattle. 9: A tough cut of beet that is below the short loin. 10. It is taken from the underside of the pig and around the stomach. 11. It refers to the cul of pork that is laken from the lop of the hind leg. 12. It refers to the meat of young sheep. 13. This cut extends below the butt towards the hock or shin of the pig. 14. It is the most tender cuts of beef. 15. Obtained from the flat lower portion of the pig, along the belly and breastbone. (Blended/Online). Access the link below for Learning Activity 6. VI. REFLECTION (Time Frame: Day 4, 10 mins) - Comrrmicate your personcal assessment as indicated in the learner's A.ssessment Using the symbols below, choose ore which besl describes your experience in working on each given lask. Drow it in the columin for Level of Performance (LP), Be guided by the deseriptions below: \( \approx-1 \) was able to do/pertorm the fosk without any difficulty, The fosk helped me in understanding the farget content/ lesson. ? - I was not able to do/perform the task. It wias extremely difficult. I need additional enrichment activitics to be able to do/p crform this tosk. \begin{tabular}{|c|c|c|c|c|c|c|c|} \hline Learning Task & LP & Learning Task & LP & Learning Task & LP & Learning Task & LP \\ \hline Number 1 & & Number 3 & & Number 5 & & Number 7 & \\ \hline Number 2 & & Number 4 & & Number 6 & & Number 8 & \\ \hline \end{tabular} Kong, Anecita P. Domo, Merlyn Lee, Maila A. Dogelio, Herry Allen M. Arcos, Ricardo Jose V. Santillan III, pages 342-343 Modules in Home Economics Cookery by: Joana C. Peralta, poges 226-233 - hiffs://www.thefreedictionary.com/cut+of+meat \begin{tabular}{|l|l|l|l|} \hline Prepared by: & Mary Joy P. Peñaloza & Checked by: & \begin{tabular}{l} Rachael D. Lusterio \\ Melinda C. Sili \\ Jennifer U. Cruz \\ Michelle B. Lopez \end{tabular} \\ \hline \end{tabular} PIVOT
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Figure $3-24$ shows the amino acid sequence of bovine insulin. This structure was determined by Frederick Sanger and his coworkers. Most of this work is described in a series of articles published in the Biochemical Journal from 1945 to 1955. When Sanger and colleagues began their work in $1945,$ it was known that insulin was a small protein consisting of two or four polypeptide chains linked by disulfide bonds. Sanger's team had developed a few simple methods for studying protein sequences. Treatment with FDNB. FDNB (1-fluoro-2,4-dinitrobenzene) reacted with free amino (but not amide or guanidinium) groups in proteins to produce dinitrophenyl (DNP) derivatives of amino acids: Acid Hydrolysis. Boiling a protein with $10 \%$ HCl for several hours hydrolyzed all of its peptide and amide bonds. Short treatments produced short polypeptides; the longer the treatment, the more complete the breakdown of the protein into its amino acids. Oxidation of Cysteines. Treatment of a protein with performic acid cleaved all the disulfide bonds and converted all Cys residues to cysteic acid residues (see Fig. $3-28$ ). Paper Chromatography. This more primitive version of thin-layer chromatography (see Fig. $10-25$ ) separated compounds based on their chemical properties, allowing identification of single amino acids and, in some cases, dipeptides. Thin-layer chromatography also separates larger peptides. As reported in his first paper (1945), Sanger reacted insulin with FDNB and hydrolyzed the resulting protein. He found many free amino acids, but only three DNP-amino acids: $a-$ DNP-glycine (DNP group attached to the $\alpha$ -amino group), $a$ -DNP-phenylalanine, and $\varepsilon$ DNP-lysine (DNP attached to the $\alpha$ -amino group). Sanger interpreted these results as showing that insulin had two protein chains: one with Gly at its amino terminus and one with Phe at its amino terminus. One of the two chains also contained a Lys residue, not at the amino terminus. He named the chain beginning with a Gly residue "A" and the chain beginning with Phe "B." (a) Explain how Sanger's results support his conclusions. (b) Are the results consistent with the known structure of bovine insulin (see Fig. 3-24) ? In a later paper ( $1949)$, Sanger described how he used these techniques to determine the first few amino acids (amino-terminal end) of each insulin chain. To analyze the B chain, for example, he carried out the following steps: 1. Oxidized insulin to separate the A and B chains. 2. Prepared a sample of pure B chain with paper chromatography. 3. Reacted the B chain with FDNB. 4. Gently acid-hydrolyzed the protein so that some small peptides would be produced. 5. Separated the DNP-peptides from the peptides that did not contain DNP groups. 6. Isolated four of the DNP-peptides, which were named B1 through B4. 7. Strongly hydrolyzed each DNP-peptide to give free amino acids. 8. Identified the amino acids in each peptide with paper chromatography. The results were as follows: B1: $ \alpha$ -DNP-phenylalanine only B2: $ \alpha$ -DNP-phenylalanine; valine B3: aspartic acid; $\alpha$ -DNP-phenylalanine; valine B4: aspartic acid; glutamic acid; $a$ -DNP-phenylalanine; valine (c) Based on these data, what are the first four (amino-terminal) amino acids of the B chain? Explain your reasoning. (d) Does this result match the known sequence of bovine insulin (Fig. $3-24$ )? Explain any discrepancies. Sanger and colleagues used these and related methods to determine the entire sequence of the A and B chains. Their sequence for the A chain was as follows: Because acid hydrolysis had converted all Asn to Asp and all Gln to Glu, these residues had to be designated Asx and Glx, respectively (exact identity in the peptide unknown). Sanger solved this problem by using protease enzymes that cleave peptide bonds, but not the amide bonds in Asn and Gln residues, to prepare short peptides. He then determined the number of amide groups present in each peptide by measuring the $\mathbf{N H}_{4}^{+}$ released when the peptide was acid-hydrolyzed. Some of the results for the A chain are shown below. The peptides may not have been completely pure, so the numbers were approximate - but good enough for Sanger's purposes. (e) Based on these data, determine the amino acid sequence of the A chain. Explain how you reached your answer. Compare it with Figure $3-24$. (TABLE CAN'T COPY)(EQUATION CAN'T COPY)
There is a huge variety of naturally occurring isoprenoids, some of which are medically or commercially important and produced industrially. The production methods include in vitro enzymatic synthesis, which is an expensive and low-yield process. In $1999,$ Wang, Oh, and Liao reported their experiments to engineer the easily grown bacterium $E .$ coli to produce large amounts of astaxanthin, a commercially important isoprenoid. Astaxanthin is a red-orange carotenoid pigment (an antioxidant) produced by marine algae. Marine animals such as shrimp, lobster, and some fish that feed on the algae get their orange color from the ingested astaxanthin. Astaxanthin is composed of eight isoprene units; its molecular formula is $\mathrm{C}_{40} \mathrm{H}_{52} \mathrm{O}_{4}$. (EQUATION CAN'T COPY) (a) Circle the eight isoprene units in the astaxanthin molecule. Hint: Use the projecting methyl groups as a guide. Astaxanthin is synthesized by the pathway shown on the next page, starting with $\Delta^{3}$ isopentenyl pyrophosphate (IPP). Steps $1$ and $2$ are shown in Figure $21-36,$ and the reaction catalyzed by IPP isomerase is shown in Figure $21-35$. (c) Briefly describe the chemical transformation in step $5$ (d) The synthesis of cholesterol (Fig. $21-37$ ) includes a cyclization (ring closure) that requires a net oxidation by $\mathrm{O}_{2}$. Does the cyclization in step $\mathrm{O}$ of the astaxanthin synthetic pathway require a net oxidation of the substrate (lycopene)? Explain your reasoning. E. coli does not make large quantities of many isoprenoids, and does not synthesize astaxanthin. It is known to synthesize small amounts of IPP, DMAPP, geranyl pyrophosphate, farnesyl pyrophosphate, and geranylgeranyl pyrophosphate. Wang and colleagues cloned several of the $E .$ coli genes that encode enzymes needed for astaxanthin synthesis, in plasmids that allowed their overexpression. These genes included idi, which encodes IPP isomerase, and $i s p A,$ which encodes a prenyl transferase that catalyzes steps 1 and 2. To engineer an $E .$ coli capable of the complete astaxanthin pathway, Wang and colleagues cloned several genes from other bacteria into plasmids that would allow their overexpression in $E .$ coli. These genes included $c r t E$ from Erwinia uredovora, which encodes an enzyme that catalyzes step $3$ and $c r t B, c r t I, c r t Y, c r t Z,$ and $c r t W$ from Agrobacterium aurantiacum, which encode enzymes for steps 4, 5, 6, 7, and 8, respectively. (EQUATION CAN'T COPY) The investigators also cloned the gene $g p s$ from Archaeoglobus fulgidus, overexpressed this gene in $E .$ coli, and extracted the gene product. When this extract was reacted with $\left[^{14} \mathrm{C}\right] \mathrm{IPP}$ and $\mathrm{DMAPP}$ or geranyl pyrophosphate or farnesyl pyrophosphate, only 14 $C-$ labeled geranylgeranyl pyrophosphate was produced in all cases. (e) Based on these data, which step(s) in the pathway are catalyzed by the enzyme encoded by gps? Explain your reasoning. Wang and coworkers then constructed several $E$. coli strains overexpressing different genes, and measured the orange color of the colonies (wild-type $E .$ coli colonies are offwhite) and the amount of astaxanthin produced (as measured by its orange color). Their results are shown below (ND indicates not determined). (TABLE CAN'T COPY) (f) Comparing the results for strains 1 through 4 with those for strains 5 through 8 , what can you conclude about the expression level of an enzyme capable of catalyzing step $3$ of the astaxanthin synthetic pathway in wild-type $E .$ coli? Explain your reasoning. (g) Based on the data above, which enzyme is rate-limiting in this pathway, IPP isomerase or the enzyme encoded by $i d i ?$ Explain your reasoning. (h) Would you expect a strain overexpressing $\mathrm{crtBIZYW}$, gps, and crtE to produce low $(+),$ medium $(++),$ or high $(+++)$ levels of astaxanthin, as measured by its orange color? Explain your reasoning.
Shows the pathway for the degradation of branched chain amino acids and the site of the biochemical defect that causes maple syrup urine disease. The initial findings that eventually led to the discovery of the defect in this disease were presented in three papers published in the late 1950s and early 1960 s. This problem traces the history of the findings from initial clinical observations to proposal of a biochemical mechanism.Menkes, Hurst, and Craig (1954) presented the cases of four siblings, all of whom died following a similar course of symptoms. In all four cases, the mother's pregnancy and the Ebirth had been normal. The first 3 to 5 days of cach child's life were also normal. But soon "thereafter each child began having convulsions, and the children died between the ages of 11 days and 3 months. Autopsy showed considerable swelling of the brain in all cases. The children's urine had a strong, unusual "maple syrup" odor, starting from about the third day of life.Menkes (1959) reported data collected from six more children. All showed symptoms similar to those described above, and died within 15 days to 20 months of birth. In one case, Menkes was able to obtain urine samples during the last months of the infant's life. When he treated the urine with 2,4 -dinitrophenylhydrazone, which forms colored precipitates with keto compounds, he found three $\alpha$ -keto acids in unusually large amounts: (EQUATIONS CAN'T COPY)(a) These $a$ -keto acids are produced by the deamination of amino acids. For each of the $a$ -keto acids above, draw and name the amino acid from which it was derived. (TABLE CAN'T COPY) Dancis, Levitz, and Westall (1960) collected further data that led them to propose the biochemical defect shown in Figure $18-28 .$ In one case, they examined a patient whose urine first showed the maple syrup odor when he was 4 months old. At the age of 10 months (March 1956 ), the child was admitted to the hospital because he had a fever, and he showed grossly retarded motor development. At the age of 20 months (January 1957 ), he was readmitted and was found to have the degenerative neurological symptoms seen in previous cases of maple syrup urine disease; he died soon after. Results of his blood and urine analyses are shown in the table on page 708 , along with normal values for each component. (b) The table includes taurine, an amino acid not normally found in proteins. Taurine is often produced as a byproduct of cell damage. Its structure is: Dancis, Levitz, and Westall (1960) collected further data that led them to propose the biochemical defect shown in Figure $18-28 .$ In one case, they examined a patient whose urine first showed the maple syrup odor when he was 4 months old. At the age of 10 months (March 1956 ), the child was admitted to the hospital because he had a fever, and he showed grossly retarded motor development. At the age of 20 months (January 1957 ), he was readmitted and was found to have the degenerative neurological symptoms seen in previous cases of maple syrup urine disease; he died soon after. Results of his blood and urine analyses are shown in the table on page 708 , along with normal values for each component. (b) The table includes taurine, an amino acid not normally found in proteins. Taurine is often produced as a byproduct of cell damage. Its structure is:Based on its structure and the information in this chapter, what is the most likely amino acid precursor of taurine? Explain your reasoning. (c) Compared with the normal values given in the table, which amino acids showed significantly elevated levels in the patient's blood in January $1957 ?$ Which ones in the patient's urine? Based on their results and their knowledge of the pathway shown in Figure $18-28$, Dancis and coauthors concluded that "although it appears most likely to the authors that the primary block is in the metabolic degradative pathway of the branched-chain amino acids, this cannot be considered established beyond question." (d) How do the data presented here support this conclusion? (e) Which data presented here do not fit this model of maple syrup urine disease? How do you explain these seemingly contradictory data? (f) What data would you need to collect to be more secure in your conclusion?
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