Dietary Protein Flashcards
Summarize the major steps in protein digestion.
- Enzymes mediate hydrolysis of proteins into single AA’s that can be absorbed
- in the stomach, pepsin is the major proteolytic enzyme
- in the small intestines, substances secreted by the pancreas further break down the partially digested material from the stomach.
- bicarbonate neutralizes the stomach acid. This raises the pH for optimal range for digestive enzymes.
- enteropeptidase cleaves typsinogen»>trypsin
- trypsin then cleaves other zymogens
Summarize the major steps in protein absorption.
Specific transport proteins transfer AAs into the intestinal cells where some are used and the rest are transported via the blood to the liver.
Describe the conversion of digestive zymogens to their active form.
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What is an essential amino acid? List them.
An amino acid that the body cannot make at all or cannot make in sufficient quantities to meet its needs.
Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Threonine Tryptophan Valine
What is the recommended protein intake?
50% carbohydrate
20% fats
30% proteins
Where is the major source of Amino acid metabolism?
liver
Other than soybeans, plant sources do not provide all the essential amino acids. Give an example of plant combinations that do.
beans + corn
beans + rice
How many calories are in a gram of protein?
4 calories
Unlike carbohydrate and fat, protein does not have a specialized form of ?
storage
If not supplied by diet, protein will be acquired from?
working and structural components of the cells and tissues
What does starvation always cause?
wasting of lean body tissue in addition to fat loss
How do you spare proteins from being used for energy and allow them to perform their unique and important roles?
Take in adequate carbohydrate and fat
In what form is pepsin secreted? Where is the zymogen stored? How is it changed?
Produced and secreted by gastric cells as pepsinogen.
HCl produced by parietal cells induces conformational change that causes pepsinogen to be cleaved to active pepsin.
What cleaves trypsinogen?
enteropeptidase
Where is enteropeptidase released?
small intestines
What would happen if enteropeptidase malfunctioned?
- trypsin would not be produced
- chymotrypsin would not be produced
- elastase would not be produced
- carboxypeptidase would not be produced
**failure to thrive, diarrhea, hypoproteinemia
Where is chymotrypsinogen synthesized?
pancreas
Where is proelastase synthesized?
pancreas
Where is procarboxypeptidase synthesized?
pancreas