CC1 PROTEIN SEMI STUDY QUESTIONS Flashcards by AGAKHAN, HANNAIS SERAINIE N.

excessive consumption of purine-rich food

ELEVATES URIC ACID

How well did you know this?

Not at all

Perfectly

harmful to cells and may decrease athletic performance.

Increased level of AMMONIA

How well did you know this?

Not at all

Perfectly

occurs when more than 2 grams per kilogram of ideal body weight per day is consumed.

Stress on KIDNEYS

How well did you know this?

Not at all

Perfectly

leads to osteoporosis, occurs with high level of protein intake

CALCIUM LOSS

How well did you know this?

Not at all

Perfectly

Two amino acids joined together by a
peptide bond form a

DIPEPTIDE

How well did you know this?

Not at all

Perfectly

activated by gastric acidity and by
autoactivation (HCL secreted by parietal cell)

Pepsinogen

How well did you know this?

Not at all

Perfectly

-hormone that stimulates the secretion of both pepsinogen and HCI

Gastrin

How well did you know this?

Not at all

Perfectly

where the enzyme pepsin is secreted by the chief cells as a proenzyme or zymogen

Gastric Phase

How well did you know this?

Not at all

Perfectly

-cleave proteins in their internal
sites

Endopeptidase

How well did you know this?

Not at all

Perfectly

stimulates the pancreas to produce a protein-free electrolyte solution
rich in bicarbonates

SECRETIN

How well did you know this?

Not at all

Perfectly

cleave one amino acid from the carboxyl-termflus of the polypeptide

carboxypeptidases

How well did you know this?

Not at all

Perfectly

Secretion of enzyme-rich pancreatic juice is mediated by the hormone

PANCREOZYMIN OR CHOLECYSTOKININ (CCK)

How well did you know this?

Not at all

Perfectly

TRYPSIN activates

-chymotrypsinogen
-pro-elastase
-procarboxypeptidase.

How well did you know this?

Not at all

Perfectly

mediated by peptidases produced
by the mucosal cells

Intestinal Phase

How well did you know this?

Not at all

Perfectly

hydrolyze the residual peptides

Aminopeptidases and dipeptidases

How well did you know this?

Not at all

Perfectly

most of the amino acids in nature are

L-AMINO ACIDS

How well did you know this?

Not at all

Perfectly

Four major groups of amino acids:

-non polar or hydrophobic
-uncharged polar
-acidic
-basic amino acids

How well did you know this?

Not at all

Perfectly

act as biologic catalysts

Enzymes

How well did you know this?

Not at all

Perfectly

the transporter across the mucosal cell membrane involves

MEISTER CYCLE

How well did you know this?

Not at all

Perfectly

PROTEINS that function for transport and storage of certain substances.

-albumin
-lipoproteins
-hemoglobin
-transferrin
-ceruloplasmin

How well did you know this?

Not at all

Perfectly

function for mechanical support

Collagen and Keratin

How well did you know this?

Not at all

Perfectly

protect the body from invading microorganisms

Immunoglobulins

How well did you know this?

Not at all

Perfectly

Cellular growth and differentiation are also controlled by

REGULATORY PROTEIN

How well did you know this?

Not at all

Perfectly

supersecondary structures called ______ are seen in the protein

MOTIFS

How well did you know this?

Not at all

Perfectly

is formed from larger domains of

tertiary structure

fundamental functional and structural unit of hydrogen bonding

DOMAIN

The plasma total proteins are within the range of

60-70 g/L or 6.0-7.8 g/d

The Nesslerization reaction involves reaction of the liberated ammonium ions with Nesssler’s reagent to form dimercuric ammonium iodide which is

yellow to orange brown

Proteins may be measured by liberating their nitrogen content using

KJELDAHL

________are sources of antibodies. On the other hand, ________ is for blood clotting

-Gamma-globulins -Fibrinogen

The total proteins include:

ALBUMIN (32-45 g/L) GLOBULIN (23-35 g/L) FIBRINOGEN (2-4 g/L).

catalyst used is

sodium nitroprusside

is measured between 540-560 nm

Purple complex

based on the ability of the peptide bonds to react with copper ions to form a purple

“biuret”complex

Among the adaptations of Biuret reaction are the

Kingsley-Biuret and Weischellboum

This method of protein determination is based on the ability of phosphotungstomolybdic acid

Folin- Ciocalteau Method

-uses Biuret method followed by the Folin-Ciocalteau’s method -This approach enhances the color obtained -More sensitive than Biuret method alone -Used to consistently obtain accurate protein determinations

Protein Lowry Assay

-used to detect peptides and amino acids after paper chromatography - sensitivity of the test is comparable with that of Coomassie dye method.

Coomassie Brilliant

Accurate levels are obtained at protein concentrations greater than 2.5 g/dL

Refractometry

example of this is the measurement of the specific gravity of blood when screening for blood donors

Specific Gravity

mostly due to the presence of tryptophan and to a lesser degree, phenylalanine and tyrosine

UV Absorption Method

-major component of the a,-globulin fraction -It acts as a protease inhibitor -It combines with and inactivate trypsin and elastase

a1-Antitrypsin (AAT)

-one of the largest non immunoglobulin proteins in the plasma. -rises tenfold or more in nephritic syndrome

a2 Macroglobulin (AMG)

-migrates in the a2-region -combines with hemoglobin released by lysis of RBC

Haptoglobin

-This is the (LDL) -migrates with a characteristic sharp leading edge and a feathery trailing edge.

B-lipoprotein

-also known as siderophilin -major B-globulin protein -transports ferric ions from iron stores

Transferrin

-travels with the B-globulins during electrophoresis -C3 is decreased in autoimmune diseases

Complement

-most abundant of the coagulation factors -increased in pregnancy and use of birth control pills -decreased during the activation of the coagulation factors -migrates between the B and y fractions -measured by the Parfentjev method

Fibrinogen

-an a2-globulin and it binds w/ copper -exhibits an oxidase activity -Deficiency of this protein is called Wilson's disease

Ceruloplasmin

-called group-specific component (Gc) globulin -binds with vitamin D -It migrates as an a,-globulin

Gc-globulin

a B-globulin and it binds with heme released from hemoglobin

Hemopexin

-also known as orosomucoid -minimize its visualization by standard protein stains

a1-acid glycoprotein

-seen in tissue necrosis -most sensitive acute phase reactant

C-reactive protein

Amino acid transport disorders:

1. Cystinuria 2. Dicarboxylic aminoaciduria 3. Hartnup diseas

Amino acid storage disease:

1. Glutaric acidemia type 2

impaired metabolism of phenylalanine

autosomal recessive

can act as poisons for people with phenylketonuria.

Aspartame

musty odor to the baby's sweat and urine due to

Phenylacetate

due to a defect in the enzyme homogentisate 1,2-dioxygenase

ALKAPTONURIA (BLACK URINE DISEASE)

-leads to a multisystemic disorder of the connective tissue, muscles, CNS, and cardiovascular system

HOMOCYSTINURIA

-body cannot effectively break down the amino acid tyrosine -Symptoms include liver and kidney disturbances and mental retardation, & can be fatal

TYROSINEMIA

most severe Tyrosinemia, caused by a deficiency of the enzyme fumarylacetoacetate hydrolase

Type 1 Tyrosinemia

-developing on the pressure points of the palm of the hand and sole of the foot -caused by a deficiency of the enzyme tyrosine aminotransferase

Tyrosinemia type Il

rare disorder caused by a deficiency of the enzyme 4- hydroxyphenylpyruvate dioxygenase

Type Ill tyrosinemia

-fish malodor syndrome -giving off a strong fishy odor or strong body odor

TRIMETHYLAMINURIA (TMAU)

affecting the proper absorption of nonpolar amino acids from the intestine and cannot reabsorb them properly from tubules

HARTNUP DISEASE (PELLAGRA-LIKE DERMATOSIS)

autosomal recessive urea cycle disorder that causes ammonia and other toxic substances to accumulate in the blood

CITRULLINEMIA /CITRULLINURIA

-ammonia builds up in the body & affected infants present lack of energy -Mutations in the ASS gene

Type 1 citrullinemia

-Characterized by confusion, aggression, irritability, and hyperactivity, seizures, and coma -It involves mutations in

Type ll citrullinemia SLC25A13 gene

-caused by mutations in the SLC341 and SLCYAS -resulting in cystine crystals & kidney stone formations

CYSTINURIA

-Characterized by defects in the ability of the body to use proteins and fats for energy, leading to acidosis -Mutations in the ETFA, ETFB, and ETFDH gene -odor of SWEATY FEET -ENLARGMENT of LIVER, HEART FAILURE

GLUTARIC ACIDEMIA TYPE 2