(a)
To determine: Whether the given statement, “Impaired
Introduction: Accumulation of metabolites such as polysaccharides or lipids in the lysosomes causes lysosomal diseases. Deficiency of certain proteins, as well as enzymes, causes the accumulation of these metabolites. Defects in proteins essential for transportation of degradation products leads to accumulation of degraded products in the lysosomes. Most lysosomal storage diseases are fatal.
(b)
To determine: Whether the given statement, “Leads to accumulation of degradation products in the lysosome” is common to most lysosomal storage diseases (M), true of a specific lysosomal storage disease (S), or not true of any lysosomal storage diseases (N).
Introduction: Accumulation of metabolites such as polysaccharides or lipids in the lysosomes causes lysosomal diseases. Deficiency of certain proteins, as well as enzymes, causes the accumulation of these metabolites. Defects in proteins essential for transportation of degradation products leads to accumulation of degraded products in the lysosomes. Most lysosomal storage diseases are fatal.
(c)
To determine: Whether the given statement, “Leads to accumulation of excessive amounts of glycogen in the lysosome” is common to most lysosomal storage diseases (M), true of a specific lysosomal storage disease (S), or not true of any lysosomal storage diseases (N).
Introduction: Accumulation of metabolites such as polysaccharides or lipids in the lysosomes causes lysosomal diseases. Deficiency of certain proteins, as well as enzymes, causes the accumulation of these metabolites. Defects in proteins essential for transportation of degradation products leads to accumulation of degraded products in the lysosomes. Most lysosomal storage diseases are fatal.
(d)
To determine: Whether the given statement, “Results from an inability to regulate the synthesis of glycosaminoglycans” is common to most lysosomal storage diseases (M), true of a specific lysosomal storage disease (S), or not true of any lysosomal storage diseases (N).
Introduction: Accumulation of metabolites such as polysaccharides or lipids in the lysosomes causes lysosomal diseases. Deficiency of certain proteins, as well as enzymes, causes the accumulation of these metabolites. Defects in proteins essential for transportation of degradation products leads to accumulation of degraded products in the lysosomes. Most lysosomal storage diseases are fatal.
(e)
To determine: Whether the given statement, “Results from an absence of functional acid hydrolases” is common to most lysosomal storage diseases (M), true of a specific lysosomal storage disease (S), or not true of any lysosomal storage diseases (N).
Introduction: Accumulation of metabolites such as polysaccharides or lipids in the lysosomes causes lysosomal diseases. Deficiency of certain proteins, as well as enzymes, causes the accumulation of these metabolites. Defects in proteins essential for transportation of degradation products leads to accumulation of degraded products in the lysosomes. Most lysosomal storage diseases are fatal.
(f)
To determine: Whether the given statement, “Results in accumulation of lysosomes in the cell” is common to most lysosomal storage diseases (M), true of a specific lysosomal storage disease (S), or not true of any lysosomal storage diseases (N).
Introduction: Accumulation of metabolites such as polysaccharides or lipids in the lysosomes causes lysosomal diseases. Deficiency of certain proteins, as well as enzymes, causes the accumulation of these metabolites. Defects in proteins essential for transportation of degradation products leads to accumulation of degraded products in the lysosomes. Most lysosomal storage diseases are fatal.
(g)
To determine: Whether the given statement, “Symptoms include muscle weakness and mental retardation” is common to most lysosomal storage diseases (M), true of a specific lysosomal storage disease (S), or not true of any lysosomal storage diseases (N).
Introduction: Accumulation of metabolites such as polysaccharides or lipids in the lysosomes causes lysosomal diseases. Deficiency of certain proteins, as well as enzymes, causes the accumulation of these metabolites. Defects in proteins essential for transportation of degradation products leads to accumulation of degraded products in the lysosomes. Most lysosomal storage diseases are fatal.
(h)
To determine: Whether the given statement, “Triggers proliferation of organelles containing catalase” is common to most lysosomal storage diseases (M), true of a specific lysosomal storage disease (S), or not true of any lysosomal storage diseases (N).
Introduction: Accumulation of metabolites such as polysaccharides or lipids in the lysosomes causes lysosomal diseases. Deficiency of certain proteins, as well as enzymes, causes the accumulation of these metabolites. Defects in proteins essential for transportation of degradation products leads to accumulation of degraded products in the lysosomes. Most lysosomal storage diseases are fatal.
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Chapter 12 Solutions
Becker's World of the Cell (9th Edition)
- If phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work?arrow_forwardHomocystinuria is caused by a defect in cystathionine beta-synthase (or 13-synthase), which leads to an accumulation of homocysteine in the blood. This accumulation causes symptoms such as a tall, thin frame, flushed cheeks, and osteoporosis (thinning of the bones). These individuals should limit their intake of proteins that contain methionine, such as egg whites. Using your understanding of biochemistry, explain why people with Homocystinuria should not consume egg whites and other such proteins.arrow_forwardHelp filling in the blanks: The malate aspartate shuttle plays many roles in carbohydrate and amino acid metabolism. Malate can be transferred into the cytosol and interconverted in one enzymatic step to produce [oxaloacetate/glucose/PEP/pyruvate] for use in the pathway of [glycolysis/gluconeogenesis]. A product of the urea cycle, derived from aspartate, can also be converted to malate in one enzymatic step and shuttled into the mitochondria so that the urea cycle product can be used in [fatty acid synthesis/the citric acid cycle/β-oxidation]. The amino group from aspartate can be transferred to [oxalacetate/malate/fumarate/pyruvate/a- ketoglutarate] to form glutamate, which is then transported into the mitochondria. In fact many amino acids are transaminated in this way to form glutamate in the cytosol. In this way, incoming amino acids from the bloodstream can be shuttled into the liver mitochondria as glutamate for conversion by glutamate dehydrogenase to [glutamate/a-ketoglutarate…arrow_forward
- i.What is mutarotation? What is the consequence of mutarotation? ii. Explain why lactose and maltose can be direct reactants in the Maillard reaction while sucrose cannot be.arrow_forwardThe “keto diet” is a dietary regimen in which carbohydrates are severely restricted, protein intake is low, and fat comprises 70–90% of daily calories. The diet causes “nutritional ketosis,” which is a different metabolic state than the ketosis that occurs in an untreated diabetic. The normal ketone body concentration is less than 0.6 mM. Explain why an individual on the keto diet may have a blood ketone body concentration of up to 3 mM. What biochemical pathways are active in an individual adhering to the keto diet? What pathways are largely inactive? Protein intake is kept low because a high-protein diet would inhibit ketosis. Explain why. Why might the keto diet lead to weight loss?arrow_forwardExplain why people with a hereditary deficiency of carnitine acyltransferase II have muscle weakness. Why are the symptoms more severe during fasting?arrow_forward
- Lysozyme’s use of aspartic acid and glutamic acid, to break the glycosidic bonds of the eubacterial cell wall (composed of peptidoglycan), illustrates the common enzymatic pattern of: hydrolysis (catabolic), using nonpolar amino acids at the active site hydrolysis (catabolic), using polar amino acids at the active site condensation (anabolic), using nonpolar amino acids at the active site condensation (anabolic), using polar amino acids at the active site all of the abovearrow_forwardThe clinical signs of two types of galactosemia—galactokinase deficiency or UDPglucose: galactose 1-phosphate uridylyltransferase deficiency—are markedly different. Although both forms cause gastrointestinal pain after drinking milk, transferase deficiency also causes liver, kidney, spleen, and brain malfunction, as well as mortality. With each kind of enzyme shortage, what products accumulate in the blood and tissues? Estimate the relative toxicity of these goods based on the information provided above.arrow_forwardExplain why people with a hereditary deficiency of carnitine acyltransferase II have muscle weakness. Why are the symptoms more severe during fasting? (Keep your answer to at least a paragraph)arrow_forward
- Phosphoribosyltransferase (PRT) catalyzes the attachment of a salvaged purine nitrogenous base on the activated form of ribose-5-phosphate called 5-phosphoribosyl- α α-pyrophosphate ( α α-PRPP). True Or Falsearrow_forwardWith fatty infiltration of the liver, the synthesis of phospholipids is disturbed. What is the biochemical basis of the development of such a condition? What are its possible nests? Justify the answer.arrow_forwardTrue or False e. Triacylglycerols and glycerophospholipids both contain fatty acids and saponifiable. True False f. Pyruvate serves as the precursor of the glycerol backbone during TAG biosynthesis. True Falsearrow_forward
- Human Heredity: Principles and Issues (MindTap Co...BiologyISBN:9781305251052Author:Michael CummingsPublisher:Cengage Learning