quiz Flashcards
Digestion of proteins begins in the _____
- stomach
what are necessary for protein hydrolysis
- pepsin
- hcl
HYDROCHLORIC ACID - acid secreted by the ______
- parietal cells
used to kill some bacteria, denature proteins, making them more susceptible to subsequent hyrolysis by the _____
proteases
used to kill some bacteria and to
denature proteins, making them more susceptible to subsequent hydrolysis by proteases
parietal cells
an acid-stable endopeptidase secreted by the ______
- serous cells
as an inactive zymogen called _____
- pepsinogen
that is activated by HCI or autocatalytically by other pepsin molecules.
- pepsinogen
Pepsin breaks down and releases ______ and a few free amino acids from dietary proteins.
peptides
On entering the small intestines, large polypeptides produced in the stomach by the action of ______ are further cleaved into _____ and amino acids
- pepsin
- oligopeptide
TRYPSIN - secreted as _____ then activated by _________
- trypsinogen
- enteropeptidase
enteropeptidase an enzyme synthesized by the _________ otherwise known as enterokinase. It hydrolyzes the polypeptide chain from the carboxyl end of ______ and _______
- intestinal mucosal cells
- arginine and lysine
plays as the common activator of all pancreatic zymogens.
- trypsin
CHYMOTRYPSIN - secreted as _____ and activated by _____ molecules.
- chymotrypsinogen
- trypsin
In chymotrypsin, It hydrolyzes the polypeptide chain from the carboxyl end of (5)
- tyrosine
- tryptophan
- phenylalanine
- met
- leucine
____ secreted as proelastase and is activated by trypsin molecules. It hydrolyzes the polypeptide chain from the carboxyl end of ______, ____, _____
- ELASTASe
- alanine
- serine
- glycine
CARBOXYPEPTIDASE A - secreted as ______ and is activated by trypsin molecules. hydrolyzes the poly peptide chain from the carboxyl end of (4)
- procarboxypeptidase A
- ala
- isoleucine
- leucine
- valine
CARBOXYPEPTIDASE B - hydrolyzes the polypeptide chain from the carboxyl end of arginine and lysine, similar to _____
myosin
______ - The luminal surface of the small intestines contains ________
- internal digestion
- aminopeptidase
an exopeptidase that repeatedly cleaves the N-terminal residue from oligopeptides to produce free amino acids and smaller peptides.
- aminopeptidase
These amino acids are absorbed mainly in ______ through the portal circulation and slightly through the _____
- small intestine
- lymphatics
amino acids enter the cells by _____
- active transport
maximum concentration in blood is attained range minutes after eating
- 30 to 50 mins
amino acid nitrogen level is kept more or less constant between __ to ___ of blood plasma.
- 4-8 mg per 100 ml
other name of nitrogen balance
equilibrium
occurs when protein intake is equal or about the same as the protein breakdown.
- nitrogen balance
This condition is typified by young adults whose protein intake is just enough to replace the daily amount of protein used.
nitrogen balance
implies a net gain of protein in the body.
- positive nitrogen balance
positive nitrogen balance - This is found whenever new tissues are being synthesized as in (3)
- growth stage
- convalescence
- pregnancy
protein intake exceeds protein output
- positive nitrogen balance
Implies greater protein utilization than protein intake, causing loss of protein from body
- negative nitrogen balance
negative nitrogen balance examples: (4)
- kwashiorkor disease
- marasmus
- lactation
- albuminuria
Inadequate intake of proteins as in fasting, diarrhea and malnutrition disorders
- kwashiorkor disease
type of malnutrition usually in children due to the inadequate intake of protein
- kwashiorkor disease
Increased catabolism of proteins as in fevers, infections and wasting diseases
- maramus
a gradual wasting away of the body, generally associated with severe malnutrition or inadequate absorption of protein and occurring mainly in young children
- maramus
increased loss of body proteins as in ___and ____
- lactation
- albuminuria
Amino acids synthesize to form proteins that are important for the body’s maintenance to life and growth.
- BIOSYNTHESIS OF NEW PROTEINS
including enzymes and hormones. The amino acids pass into systemic blood to the different organs and are used as building blocks
- tissue PROTEINS
like plasma albumin, globulin, and fibrinogen where the liver is the primary site for their biosynthesis
- plasma protein
is important for the optimal strusture and function of some important organs like liver, intestines and kidneys
- labile protein
The alpha-amino groups from amino acids are the precursors in the biosynthesis of (2) bases of the nucleotides, porphyrins, creatine, neurotransmitters and other nitrogenous compounds.
- purine
- pyrimidine
The catabolism of amino acids follow varied metabolic pathways.
- AMINO ACID CATABOLISM
AMINO ACID CATABOLISM (3)
- DECARBOXYLATION
- transamination
- OXIDATIVE DEAMINATION
enzyme in decarboxylation
- decarboxylase
refers to the removal of the carboxyl group of the amino acid for the formation of a physiologic active amine
- decarboxylation
refers to the removal of the amino group that begins with the transfer of this amino group to an amino group acceptor.
- transamination
usually ________ that eventually turns into glutamate
- alpha-ketoglutarate (transamination)
transamination is catalyzed by
- transaminase
After transamination, the amino acid tums into an _____
- alpha - keto acid or a carbon skeleton
It turns into acetyl-coA, pyruvate or other intermediates and is oxidized to produce biochemical energy (ATP) via the Kreb’s cycle with the release of (2)
- carbon dioxide and water (transamination)
it is converted into a carbohydrate or fat molecule
- transamination
It is reaminated to form amino acids
- transamination
this substance undergoes oxidative deamination to reform alpha-ketoglutarate and release
- ammonia (NH3)
once the amino groups have all been collected in the form of glutamate
- OXIDATIVE DEAMINATION
once the amino groups have all been collected in the form of _______
glutamate
It is utilized for the synthesis of non-protein nitrogenous compounds
- OXIDATIVE DEAMINATION
It enters the ornithine cycle for the formation of ______
- urea
It is detoxified for the synthesis of ______
glutamine
3 processes of amino acid catabolism
- decarboxylation
- transamination
- oxidative deamination
refers to the removal of the carboxyl group of the amino acid for the formation of a physiologic active amine
- decarboxylation
refers to the removal of the amino group that begins with the transfer of this amino group to an amino group acceptor.
- transamination
usually ________ that eventually turns into glutamate.
alpha-ketoglutarate (transamination
UPAC name for DOPA
- (L-3,4- dihydroxyphenylalanine)
due to the absence of the enzyme of tyrosinase
- albinism
ALBINISM - due to the absence of the enzyme of
- tyrosinase
There is also abnormal pigmentation of cartilages, fibrous tissues and tendons, an abnormal condition known as
- ochronosis
When the urine containing homogentesic acid is exposed to the atmosphere turn to what color
black (due to oxidation)
an iron containing enzyme which catalyzes the oxidation of homogentisic acid to fumarate and acetate.
- homogentisic acid oxygenase
ALKAPTONURIA - due to the absence of
- homogentisic acid oxygenase
hydroxyphenylpyruvic acid is not oxidized into
- homogentesic acid
the absence of hydroxyphenylpyruvic acid oxidase
- TYROSINOSIS
is instead converted into phenylpyruvic acid which impairs normal development of child’s brain leading to mental retardation.
- phenylalanine
due to the absence of the enzyme phenylalanine hydroxydase which converts phenylalanine to ______
- tyrosine
absence of the enzyme in PHENYLPYRUVIC OLIGOPHRENIA
- phenylalanine hydroxydase
other name of phenylketonuria
- PHENYLPYRUVIC OLIGOPHRENIA
These intermediates are substrates for gluconeogenesis and can give rise to the net formation of glycogen in liver and muscle.
- Glucogenic amino acids
one of the intermediates of the citric acid cycle.
- pyruvate
Glucogenic amino acids are amino acids whose catabolism yields _____
- pyruvate
only exclusively ketogenic amino acids found in proteins.
- lysine
- leucine
are amino acids whose catabolism yields either acetoacetate or one of its precursors, acetyl CoA or acetoacetyl CoA
- Ketogenic amino acids
The catabolism of the carbon skeletons converges to form ____ products, which is the basis of classifying amino acids based on the nature of their metabolic end products
- seven
The catabolism of the 20 amino acids found in proteins involves the removal of alpha-amino groups followed by the breakdown of the resulting _____
carbon skeleton
The catabolism of the 20 amino acids found in proteins involves the removal of _____ followed by the breakdown of the resulting
- alpha-amino groups