christopherc63

Axcel Software began a new development project in 2015. Theproject reached technological feasibility on June 30, 2016, and wasavailable for release to customers at the beginning of 2017.Development costs incurred prior to June 30, 2016, were $3,200,000and costs incurred from June 30 to the product release date were$1,400,000. The 2017 revenues from the sale of the new softwarewere $4,000,000, and the company anticipates additional revenues of$6,000,000. The economic life of the software is estimated at fouryears. Capitalized software costs are:

Hello I have 44 questions

What is 69+420?

Who is Zayn Malik?

When is the number of different chromosomes in a cell divided inhalf?

there aren't health risks with any yoga positions or forms.

how often does a 16-year-old need a medical evaluation from a doctor?

which of the following are symptoms of influenza infection?

which nursing intervention is most appropriate for a client with multiple myeloma?

using a nicotine patch for smoking cessation is an example of which route of administration?

the cns depressants include various prescription drugs referred to as

it's always safer to exercise in a gym.

medical technician

morgue assistant

yoga instructor

medical director job descriptions

Complementation epistasis produces a phenotypic ratio of

9:3:4

9:7

15:1

13:3

9:3:3:1

The answer is 9:7 so i'd like to know why and what exactly complemenation epistasis is?

#7

1.

Of what value is deamination to a microbe?

2.

What causes the black precipitate in a pos

itive H

3

S test? What does it indicate about the

metabolism of the organism?

4.

Kligler’s iron agar is a multitest medium. Explain the meaning of this statement.

5.

Explain how Kligler’s iron agar allows differentiation between bacteria that can ferme

nt

glucose and those that can ferment lactose.

What results will be observed in Kligler's agar medium for a bacterium that can ferment glucose and lactose? What results will be observed for a bacterium that can ferment glucose but not lactose? Briefly explain the biochemical reason for the difference between these two results.

Biochem:

1

1. Identify if the following enzymes in the liver are active,inactive or unaffected during fasting

a. Branching Enzyme -

b. Debranching Enzyme -

c. Glycogen Synthase -

d. Glycogen Phosphorylase -

e. Glucokinase -

2. Explain the outcomes of each of the following GlycogenStorage Diseases

a. Lack of Debranching Enzyme -

b. Lack of Muscle Glycogen –

c. Lack of Glut-2 transporters -

d. Lack of Branching Enzyme –

e. Lack of Liver Glycogen Synthase -

f. Lack of Glucose-6-Phosphatase -

g. Lack of Liver Glycogen –

3. Explain why Branching Enzyme and Debranching Enzyme areneeded in glycogen metabolism.

4. Suppose a mutation occurs in Phosphoglucomutase which doesnot allow the enzyme to catalyze the movement of the phosphategroup from the 6 position of glucose to the 1 position. What wouldbe the effects of this mutation in Glycogen metabolism?

2

4. Suppose a mutation occurs in Phosphoglucomutase which doesnot allow the enzyme to catalyze the movement of the phosphategroup from the 6 position of glucose to the 1 position. What wouldbe the effects of this mutation in Glycogen metabolism?

5. Liver glycogen is used in fasting to provide glucose for useby other tissues including the brain. Muscle glycogen is not. Whatis the explanation for this?

2

4. Suppose a mutation occurs in Phosphoglucomutase which doesnot allow the enzyme to catalyze the movement of the phosphategroup from the 6 position of glucose to the 1 position. What wouldbe the effects of this mutation in Glycogen metabolism?

5. Liver glycogen is used in fasting to provide glucose for useby other tissues including the brain. Muscle glycogen is not. Whatis the explanation for this?

6. Which of the following statements about the control ofglycogen synthase are correct? Select all that apply.

a) Glycogen synthase is inactivated by a proteinphosphatase.

b) Glycogen synthase is activated in the presence ofinsulin.

c) PKA and glycogen synthase kinase 3 phosphorylate glycogensynthase at different sites.

d) The phosphorylation by glycogen synthase kinase 3 isinhibited by insulin.

e) Insulin activates protein kinase B which phosphorylatesglycogen synthase.

Questions from study guide for biochem exam. Please answer as many as you can. Thank you

1. Where is glycogen found? What is the glycogen granule comprised of and what is its overall structure? What types of linkages are found in glycogen? How do they differ from cellulose?

2. What is glycogen phosphorylase? What are the two activities of the debranching enzyme? What does phosphoglucomutase do in both breakdown and synthesis of the glycogen particle? What are the two products of glycogen breakdown? In what proportion will they be found?

3. What is UDP-glucose pyrophosphorylase and what does it do? What is glycogen synthase? What is glycogenin?

4. What signals lead to the breakdown/synthesis of glycogen?

5. When is phosphorylase active/inactive? When is glycogen synthase active/inactive? What role do phosphorylase kinase, PP1c, GSK-3, and the GL or GM proteins play in regulation of glycogen synthesis/breakdown?

6. What role does Ca2+ and AMP play in the breakdown of glycogen in the skeletal muscle?

7. Based on the questions above (#4-6) you should be prepared to fully diagram the regulation of glycogen synthesis and breakdown.

A typical glycogen particle contains 50,000 glucose residues and has 2,000 non-reducing ends. Recall that the degradation of glycogen involves the action of glycogen phosphorylase, which releases glucose 1-P, and glycogen debranching enzyme, which releases glucose.

A - Approximately how many ATP’s are produced from the complete catabolism of one glycogen particle?

B - The addition of one glucose residue onto the nonreducing end of a glycogen strand requires six enzymes: hexokinase; phosphoglucomutase; UDP-glucose pyrophosphorylase; inorganic pyrophosphatase; glycogen synthase; and nucleoside diphosphate kinase. By considering the net reaction catalyzed by the sequential action of these enzymes, determine how many ATP’s are required to add one glucose molecule onto glycogen, and from that, how many ATP’s are required to synthesize an entire glycogen particle.

C - Given that 31 ATP molecules are produced from each glucose 6-P through oxidative phosphorylation, compare the cost of production of a glycogen particle and the energy obtained by its complete oxidation to calculate the efficiency of storing glucose in glycogen. The efficiency can be considered to be (net ATP gained)/(total ATP gained).

Does anyone know Biochem Please help!!!Some questions may have more than on answer...............

2a A liver cell with high cellular ATP and low cytosolic glucose is exporting glucose in response to stimulation by glucagon. CHOOSE ALL(this means more than one answer may be selected) of the following that are consistent with these cellular conditions.

a. glycogen phosphorylase breaks a(1,4) glycosidic bond of glucose residues on the non-reducing ends of glycogen

b. the rate of glycogen synthase is inibited

c. the rate of glycolysis is inhibited

d.the caalytic rate of phosphofructokinase is inhibited by ATP

e the rate of glycogen phosphorylase by ATP

2b..In a muscle or a liver cell, stimulation by hormone adrenaline, leads to________. CHOOSE ALL(that means more than one) of the following that are consistent with these cellular conditions.

a. an increase in the glycogen phosphorylase a form of the enzyme

b. an increase in glycogen synthase a form of enzyme

c. increase in phosphorylation of glycogen phosphorylase

d. increase in phosphorylation of glycogen synthase

2c.In exercising muscle cells the cellular AMP concentration is high the cell is stimulated by adrenaline. CHOOSE ALL(that means more than one) of the following that are consistent with these cellular conditions.

a. Glycogen phosphorylase is in the form of phosphorylase b

b. Glycogen synthase is in the form of synrhaseb

c The glycolysis rate is stimulated

d. Net glycogen breakdown takes place

e. AMP stimulates the rate of glucose export

f. AMP stimulate the catalytic rate of phosphofructofinase

1. How many ATP's are required to add one glucose unit to glycogen?

2.A typical glycogen particle has 55,000 glucose residues and 2,000 non-reducing ends. Determine the total number of ATP's that are produced through glycolysis when a glycogen particle is completely degraded by glycogen phosphorylase and glycogen debranching enzyme.

What role do vitamins have in the pyruvate dehydrogenase reaction? There are FOUR correct answers.

A.Riboflavin is an electron carrier that functions in a redox reaction involving dihydrolipoamide.

B. Most children in developed countries have defective PDH protein complexes and suffer from malnourishment because they eat too much Captain Crunch cereal and not enough broccoli, asparagus, and brown rice.

C. Vitamin B5 functions as an acetate carrier using a high energy thioester bond formed in the E2 catalytic site.

D. One of the reasons why people get beriberi when their diets are lacking in vitamin B1 is that the PDH reaction becomes overstimulated and high levels of acetyl-CoA are toxic.

E. Thiamin pyrophosphate transfers a pair of electrons from E2 to E3, which in turn, oxidizes NAD+ to generate NADH + H+.

F. Vitamin B3 is a critical component of not only the PDH complex, but also the alpha-ketoglutarate dehydrogenase complex, an enzyme in the citrate cycle.

G.Vitamins provide functional chemical groups in all three subunits of the PDH protein complex.

You have perfected a procedure in which the two enzyme complexes pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase can be dissociated into their individual subunits and the subunits then reassembled into “holoenzymes.” Which protein subunit could be “swapped” between pyruvate dehydrogenase and alpha-keto glutarate dehydrogenase without loss of activity to either reconstituted enzyme when each of the enzyme complexes is provided with its appropriate substrate?

Consider the route for alanine catabolism when choosing an answer. (please help!)

Can someone please check my answers?

1. The amide nitrogen of glutamine:

A. represents a nontoxic transport form of ammonia.

B. is a major source of ammonia for urinary excretion.

C. is used in the synthesis of asparagine, purines, and pynimidines.

D. can be recovered as ammonia by the action of glutaminase.

E. all of the above are correct.

2- Which of the following statements about glutamate is NOT true:

a It can be synthesized in the transaminase reaction using alanine as a substrate

b It can be synthesized in an aminotransferase reaction using aspartate as a substrate

c It can be synthesized by the glutamate dehydrogenase reaction using alpha-ketoglutarate and free ammonium ion as substrates

d It can transfer it's amino group to oxaloacetate in a one step reaction

e It can transfer it's amino group to citrulline in a one step reaction

3. The products of the catabolism of cysteine are:

a) Serine and phosphate

b) Serine and HCl

c) Pyruvate and sulfate

d) Serine and sulfate

e) Alanine and sulfate

4. The catabolic products of isoleucine, methionine, and valine all enter into the TCA cycle or glycolysis as

A Pyruvate

B Oxaloacetate

C Succinyl CoA

D Acetyl CoA

E Fumarate

5-What is the name of the cofactor for AST, ALT, or any other transamination reaction?

A NAD⁺

B Acetyl CoA

C Pyridoxal phosphate (PLP)

D FADH₂

E NADPH

6. Valine and isoleucine give rise to propionyl CoA, a precursor succinyl CoA. A disease related to a defect in this conversion methylmalonic aciduria. Some patients respond to megadoses of vitamin B Which of the following statements about the conversion of propionyl CoA to succinyl CoA is/are correct?

A. The first step in the conversion is a biotin-dependent carboxylation.

B. Some methylmalonic aciduria patients respond to B12 because the defect in the mutase converting malonyl CoA to succinyl CoA is poor binding of the cofactor.

C. The same pathway of propionyl CoA to succinyl CoA is part oa the metabolism of odd-chain fatty acids.

D. All of the above are correct.

E. None of the above is correct.

7. All of the following are true about the branched-chain amino acids EXCEPT:

A. they are essential in the diet.

B. they differ in that one is glucogenic, one is ketogenic, and one is classified as both.

C. they are catabolized in a manner that bears a resemblance to B-oxidation of fatty acids.

D. they are oxidized by a dehydrogenase complex to branch chain acyl CoAs one carbon shorter than the parent compound.

E. they are metabolized initially in the liver.

8-The most dramatic increases in serum alanine transaminase(SGPT or ALT) levels occur in patients with

A. biliary obstruction.

B. hemolysis.

C. malabsorption of fat-soluble vitamins.

D. inflammatory diseases of the liver.

E. intrahepatic cholestasis.

9. S-Adenosylmethionine:

A. contains a positively charged sulfur (sulfonium) that facilitates the transfer of substituents to suitable acceptors.

B. yields a-ketobutyrate in the reaction in which the methyl is transferred.

C. donates a methyl group in a freely reversible reaction.

D. generates H2S by transsulfuration.

E. provides the carbons for the formation of cysteine.

10-Which of the following compounds serves as a coenzyme for transaminase reactions?

A. pyridoxal phosphate

B. thiamine pyrophosphate

C. nicotinamide adenine dinucleotide

D. flavin adenine dinucleotide

E. coenzyme A

11. In transamination, which amino acid is converted into oxaloacetic acid?
A. Lysine
B. Aspartic
C. Glutamic
D. Threonine
E. Methionine

12.The a -keto acid that is produced by transamination of alanine is:

A. oxalic acid

B. pyruvic acid

C. oxaloacetic acid

D. a -keto butyric acid

E. homocysteine

13- The reactions of the urea cycle take place in

a) the cytosol.

b) the mitochondrion.

c) the nucleus.

d) the cytosol and the mitochondrion.

e) the cytosol and the nucleus.

14- Intermediates in the urea cycle include all of the following except

a) lysine.

b) ornithine.

c) arginine.

d) citrulline.

e) carbamoyl phosphate.

15- The nitrogen atoms in urea are derived directly from

a) ammonia and lysine.

b) ammonia and aspartate.

c) glutamine and glutamate.

d) glycine and ammonia.

e) glycine and asparagine.

16. Carbamoyl phosphate synthetase I:

A. is a flavoprotein.

B. is controlled primarily by feedback inhibition.

C. is unresponsive to changes in arginine.

D. requires N-acetylglutamate as an allosteric effector.

E. requires ATP as an allosteric effector.

17- Which one of the following is synthesized from an essential amino acid?

A. Alanine

B. Glutamate

C. Proline

D. Tyrosine

E. Aspartate

18. The step in porphyrin biosynthesis which is excessively stimulated in the acute porphyrias is the step catalyzed by

A. delta-amino levulinic acid synthase

B. uroporphyrinogen III cosynthase

C. porphobilinogen deaminase

D. coproporphyrinogen III oxidase

E. ferrochelatase

19.In jaundice that accompanies neonatal isoimmune hemolysis the substance most likely to be elevated in serum is

A. beta-glucuronidase.

B. bilirubin diglucuronide.

C. biliverdin.

D. unconjugated bilirubin.

E. deoxycholic acid.

20. Increased excretion of urobilinogen in the urine is generally the result of

A. acute hemolytic anemia.

B. erythropoetic porphyria.

C. Gilbert’s syndrome.

D. iron deficiency.

E. bile duct obstruction.

The following is a list of hereditary metabolic defects involvingloss of single enzymes of catabolism, and a second list of possibleconsequences. Match each enzyme with its most likely (only one)consequence from the list.

DEFECTS:
a. lack of phosphoglucomutase
b. lack of triose phosphate isomerase
c. lack of phosphofructokinase
d. lack of glycogen phosphorylase kinase
e. lack of phosphorylase a phosphatase
f. lack of isocitrate dehydrogenase
g. lack of pyruvate dehydrogenase

CONSEQUENCES:
1. Inability to use glycogen as an energy source, with no effect onability to use galactose
2. lethal; prevents use of carbohydrates for ATP production
3. impaired ability to obtain energy from carbohydrates
4. Lethal; prevents complete oxidation of all fuel molecules
5. A lower than normal steady state level of glycogen
6. Inability to use glycogen or galactose as an energy source
7.Inability to obtain energy from carbohydrates, and impairedability to obtain energy from amino acids


Please explain the answers in a thorough manner.

The following is a list of hereditary metabolic defectsinvolving loss of single enzymes of catabolism, and a second listof possible consequences of such defects. Match each enzyme withits most likely consequence (only one).

- what is the structure of glycogen?

- What is the overall scheme for glycogen breakdown (aka glycogenolysis)? (include phosphorylase, debranching enzyme, 1,6-glucosidase, phosphoglucomutase)

32a. What is the role of starch phosphorylase in starch degradation?

b. What is the role of debranching enzyme?

c. What is the role of glucosyltransferase?

33a. What is the role of amylase (both α and β) in starch degradation?

b. What is the role of α-glucosidase in starch degradation?

c. Why can’t hydrolytic enzymes completely convert starch to hexose?

1. Using the multiplication rule, calculate the probabilities of each genotype occurring from a given cross.

2. Using the multiplication rule and the addition rule, calculate the probabilities of a certain combination of genotypes occurring as the result of a genetic cross.

3. Distinguish between incomplete dominance and codominance, multiple alleles and pleiotropy, epistasis and polygenic inheritance.

4. Explain how each of the following impact the phenotype; incomplete dominance, codominance, multiple alleles, pleiotropy, epistasis, polygenic inheritance, environmental influence.

5. Explain the role of the environment in the phenotypic range of some genes.

5. Describe or recognize examples of the various modes of inheritance: complete dominance, incomplete dominance, codominance, multiple alleles, pleiotropy, polygenic, epigenetic, and X or Y-linked (sex linked).

6. Solve genetics problems (i.e., determine offspring phenotypic and/or genotypic ratios, mode of inheritance, parental genotypes and/or phenotypes) involving genes exhibiting complete dominance, incomplete dominance, codominance, multiple alleles, pleiotropy, and X-linkage (sex linkage).

7. Describe the purpose of a testcross and suggest an appropriate genotype and phenotype for performing a testcross given appropriate information. Interpret the results of a testcross.

8. Interpret pedigrees and determine the most likely mode of inheritance supported by the pedigree. Predict the genotype or phenotype of individuals within the pedigree