ch. 6 Proteins

Skeletal and cardiac muscle

Where are branched chained amino acids primarily used?

Central carbon, carboxyl acid group, amino group, and a side chain

What is apart of the general structure of an amino acid?

The stomach

Where is pepsinogen converted and used?

Pepsin

What is pepsinogen converted to?

Elevated blood ammonia

What can be observed with advanced liver disease

Animal sources

Where can good quality proteins come from in a diet?

False

True or false: casein is a fast protein

True

True or false: creatine can be synthesized in the body

False

True or false: creatine must be obtained through the diet

Trauma and/or infection

What increases glutamine uses (by cells) in the body

Autophagy-Lysosome System, ubiquities proteasomal pathway, and calpains

What are the ways proteins can be degraded?

Sarcopenia

In older adults, what can cause a decrease in the metabolic rate?

Net charge, structure, polarity, and essentiality

How can an amino acid be classified?

Proteolytic

Pertaining to the breakdown of protein

endopeptidase

An enzyme the hydrolyzes amino acids linked to other amino acids in the interior of a peptide or protein

Phagocytosis

An endocytotic process in which material is engulfed into a cell

Transport proteins

Proteins that transport nutrients in blood or into and out of cells or cell organelles

Osmotic pressure

A property of a solution that is proportional to the nondiffusible solute concentration

Autophagy

The breakdown or digestion of the body's proteins, such as those found in the blood or within cells

Proteoglycans

Large molecules made up of proteins and glycosaminoglycans

Cathepsins

A group of enzymes involved in breaking down or digesting the body's proteins

Complete protein

A protein that contains all the essential (indispensable) amino acids in the approximate amounts needed by humans

marasmus

Malnutrition caused by prolonged intake of a diet deficient in energy (kcal)

Phenylalanine

Which amino acid contains an aromatic ring

Lysine

Which amino acid has a positively charged side group

Intestine

Trypsin is a digestive enzyme that is most active in the _________?

Glutamate and aspartate

The most slowly absorbed amino acids are

Liver

After you eat a meal, the majority of the amino acids consumed are taken up by the

Aspartate aminotransferase

Bill suffered heart damage as a result of a heart attack. Which of the following enzymes was likely elevated after he sustained damage to his heart

Ammonia

The Kerbs cycle is critical for the removal of _____ from the body

Tyrosine

The neurotransmitter, dopamine, is synthesized from which amino acid

Physical activity

Protein synthesis can be enhanced by

Insulin and leucine

Two factors that influence the activity of mTOR are

Supply of intermediates for the TCA cycle

Which function is glutamine least involved with in the body

Glutathione

An example of a nitrogen -containing non-protein compound that plays a role as an indicator of a cell’s redox state is

Enters the portal blood

After proline is synthesized in the intestinal cell from pyrroline 5-carboxylate, it ______

ATP

Unfolding the secondary and tertiary structure of ubiquitinated proteins requires

Eggs

An example of a complete protein is

Protein

Dark brown, foamy urine is likely an indication of an abnormal amount of

Tertiary

Albumin is a globular protein. This means that it has a _____ structure containing multiple alpha helices and beta pleated sheets

Painful joints

Unit acid produced as a byproduct of the purine degradation can build up in the body of renal failure patients. What symptoms may result from this process

Tubules

Elevated urinary glucose can occur when patient's kidneys are failing due to the inability of the ______ to reabsorb filtered glucose

Amount of nitrogen (glutamine has 2 nitrogens and glutamic acid has 1 )

What is the difference between glutamine and its acid form? - lecture

Morbidity and mortality

Malnutrition is associated with an increase in what?

Marasmus

What does a chronic or prolonged reduced access of food result in?

Age, body size, and physiological state

What are protein and amino acid requirements for humans influenced by?

0.66 g of protein per kg of body weight OR 105 mg of nitrogen

What is the Estimated Average Requirement for adults for protein?

0.8 g of protein per kg of body weight

What is the recommended Dietary Allowance for protein for adults?

None

What Tolerable Upper Intake Level for protein has been established

Grains - should be high in fiber

What food group also provides protein

True

True or false: higher amounts of plant foods need to be eaten to obtain sufficient amounts of protein

Nitrogen intake

Protein intake is the base of the assessment of what

Casein

What does the FDA use as the standard comparison of protein based on PER

Casein, whey

Cow milk is 80% _ and 20% _

PDCAAS - protein digestibility corrected amino acid score

What is the commonly used indicator of protein quality

Preschool children

What age group has the highest recommended requirements for amino acids?

DIAAS - digestible indispensable amino acid score

What is the newer method to assess protein quality

Zwitterion

Amino acids with no side chain generating an additional charge

Aspartate and glutamate

What is aspartic acid and glutamic acid with a net negative charge called

Lysine, arginine, histidine

What are the basic amino acids with a net positive charge

Side chain (R group)

What does the polarity of an amino acid depend on

Indispensable

What is another term for essential amino acids

Leucine, isoleucine, valines, lysine, tryptophan, threonine, methionine, phenylalanine, and histidine

What are the 9 indispensable amino acids for adult humans

Cirrhosis - liver disease or immature liver function

______ impairs phenylalanine and methionine metabolism