Protein

MAHATHIR ALPHA · 55問 · 2年前

通報

問題一覧

Built from one or more chains of amino acids

Protein

What does Protein contain?

Contain carbon, hydrogen, oxygen, sulfur and nitrogen

It dictates the amino acid sequence of the protein

Nucleotide sequence

Immunoglobulins are made in _________.

Plasma cells

Insufficient dietary quantities of ____________ will limit synthesis and lower body levels of proteins

amino acids

The end product of protein catabolism

To remove nitrogen from the system

It occurs in the digestive tract, kidneys, and liver – which produces ammonia then urea.

Protein catabolism

They increase protein synthesis

Growth hormone Insulin

They increase protein catabolism

Glucocorticoids Thyroid hormone

It is determined by which amino acids are present, the arrangement of the 20 amino acids in the polypeptide their sequence and the number of amino acids. One amino acid substitution can alter biologic activity, even in a large protein.

Primary structure

It is the shape the strand of amino acids takes as amino acids interact with adjacent amino acids through hydrogen bonds, disulfide linkages between the cysteine amino acids and other polar and nonpolar R group interactions. The peptide bond does not rotate much, but other bonds are free to rotate. This rotation allows conformational changes that cause the secondary shape to form

Secondary structure

Give the shapes under secondary structure

Alpha-helix Beta pleated sheath No apparent pattern

Coil or ring

Alpha-helix

Flat or corrugated

Beta pleated sheath

Random (secondary structure)

No apparent pattern

It is the three–dimensional structure that forms as the amino acids interact with more distant members of the chain causing the chain to fold and takes its characteristic shape.

Tertiary structure

It is formed when two or more chains are united. These chains are called monomers or subunits and the final proteins formed are called dimers, tetramers or oligomers.

Quaternary structure

Give out the Classification of Proteins

Simple protein Conjugated protein

What are the types of simple protein?

Globular protein Fibrous protein

What are the types of Conjugated proteins?

Chromoprotein Metalloprotein Lipoprotein Glycoprotein Nucleoproteins

This type of protein have a ratio of less than 10. A length to breath ratio closer to 2 or 3. e.g. hormones, enzymes, hemoproteins

Globular proteins

This type of protein have a ratio greater than 10. e.g. myosin, keratin

Fibrous proteins

This type of protein contain an organic prosthetic group that is linked to some metal ions. e.g. Myoglobin, hemoglobin

Chromoprotein

This type of protein have some metal ions that are directly attached to the protein. e.g. Ferritin, ceruloplasmin

Metalloprotein

This type of protein contain bound cholesterol, phospholipid or both.

Lipoprotein

This type of protein contain complex carbohydrate in their structure e.g. Mucin and crossomucoid

Glycoprotein

This type of protein is associated with chains of DNA.

Nucleoproteins

What are the types of protein according to solubility?

Albumin Globulin Albuminoids

These proteins that are soluble in water and soluble in dilute and concentrated salt solutions but insoluble in highly concentrated salt solutions such as saturated ammonium sulfate.

Albumin

These are proteins that are insoluble in water, soluble in weak neutral salt solutions but insoluble in concentrated salt solutions.

Globulin

A special group of proteins characterized by being essentially insoluble in some common reagents. e.g. collagen, elastin, keratin

Albuminoids

Give examples of plasma proteins

Albumin Globulins Fibrinogen

-Synthesized mainly in the liver -Migrates ahead of albumin on electrophoresis -Transport protein for thyroid hormones and retinol(Vitamin A)

Plasma Proteins

-Synthesized in the liver, -Soluble in water and dilute and concentrated salt solutions but insoluble in highly concentrated solutions -Protein present in the highest concentration in the plasma

Albumin

It is a protease inhibitor that neutralizes trypsin- type enzymes that can damage structural proteins

α1- Anti trypsin

It is synthesized during gestation in the yolk sac and liver of the fetus

α – Fetoprotein

It is an α2 - globulin that binds free hemoglobin

Haptoglobin a

It is an α2 - globulin copper containing protein

Ceruloplasmin

It is a proteolytic enzyme that inhibits thrombin, trypsin and pepsin.

α2 -Macroglobulin

a β- globulin that transport iron

Transferrin

Antibodies – synthesized in the plasma cells as an immune

Immunoglobulins

It is used to predict risk of premature birth

Fibronectin

Digestion of protein begins in the __________ immediately after ingestion. Gastric secretion includes hydrochloric acid and pepsin.

Stomach

It acts specifically on the peptide bonds between those amino acids containing an aromatic ring or carboxylic acid in their R group, breaking the proteins into shorter polypeptides. As the polypeptide move into small intestine, the pH changes from acidic to basic and pepsin in inactivated.

Pepsin

It acts on the peptide bonds between the amino acids with basic R group.

Trypsin

It breaks the peptide bonds between amino acids with neutral R groups

Chymotrypsin

It acts on bond between the small amino acids such as glycine, alanine and serine.

Elastase

It attacks the carboxyl terminal amino acid, liberating amino acids one at a time.

Carboxypeptidase

It is secreted by the small intestine, acts on the amino terminal end to force single amino acids.

Aminopeptidase

True/False: Albumin, alpha and beta globulins, prothrombin and fibrinogen are all formed in the liver.

True

They are formed in the liver and in all reticuloendothelial tissues of the body

Gamma globulins

A process known as ______________ takes place in the body wherein proteins are degraded and resynthesized to be distributed in other parts of the body.

Protein turnover

It is the disruption of the bonds holding the secondary, tertiary or quaternary structure

Denaturation or inactivation

Denaturation or inactivation is accomplished by:

Heat Ph changes Chemicals Mechanical factor

Heart marker for Ml

Myoglobin Troponin

Distinguishes between MI and CHF

BNP

Glycoprotein used to predict the short-term risk of premature delivery

Fibronectin

Total protein level < 6.4 g/Dl

Hypoproteinemia

Total protein level > 8.3 g/dL

Hyperproteinemia

Excess water loss leads to the increased concentration of proteins

Dehydration

-Linked together by peptide bonds to form the building blocks of proteins -Building blocks of proteins

Amino Acids

-Rare inherited disorders -Enzyme defect that inhibits the body’s ability to metabolize certain amino acids -Abnormality due to problem with enzyme activity or the membrane transport system for amino acids -Cause severe medical problems due to the buildup of toxic amino acids and/or byproducts of amino acidmetabolism in blood

Aminoacidopathies

-Absence of phenylalanine -Hydrolase giving Mousy odor of the urine -Causes significant brain damage

Phenylketonuria

-Three types -Type I most severe -Causes liver and kidney damage, affects CNS

Tyrosinemia

-Absence of homogentisate oxidase -Urine turns brownish-black upon exposure to air

Alkaptonuria

-Absence or reduction of alpha-ketoacid decarboxylase -Hallmark feature is the odor of maple syrup or burnt sugar in the urine, breath and skin

Maple syrup urine disease

-Absence of isovaleric-CoA dehydrogenase -Distinctive odor of sweaty feet due to build up of isovaleric acid

Isovaleric Acidemia

Absence of cystathionine-beta synthetase

Homocystinuria

-Defect in amino acid transport system -Results in the formation of stones

Cystinuria

Reference range for total protein

6.4- 8.3 g/dL

Digestion of protein; measurement of nitrogen content

Kjeldahl

Measurement of refractive index due to solutes in serum

Refractometry

Formation of violet-colored chelate between Cu2+ ions and peptide bonds

Biuret

Protein binds to dye and causes a spectral shift in the absorbance maximum of the dye

Dye bonding

It is for the identification of monoclonal spikes of immunoglobulins and differentiating them from polyclonal hypergammaglobulinemia.

Serum protein electrophoresis(SPE)

It produces a pattern of acute inflammation associated with tissue injury- elevated acute phase reactants (AAT, haptoglobin, alpha-1 antichymotrypsin).

Myocardial infarction

READ! Normal SPE Pattern: 1. Albumin- fastest band; 1st band 2. Alpha 1- Globulin (2nd fastest band) Increase as a non-specific response to inflammation Glycoproteins, AAT, AAG, thyroxine binding-globulin (TBG) 3. Alpha 2-Globulin (3rd band fastest band) Haptoglobin, AMG, ceruloplasmin 4. Beta- globulin (4th band) Transferrin, beta-lipoprotein, hemopexin, complement system (C3 and C4) 5. Gamma-globulin (Immunoglobulin) Slowest band; 5th band

READ! Abnormal Serum Electrophoretic Patterns: 1. Gamma spike - multiple myeloma 2. Beta- gamma bridging - hepatic cirrhosis 3. a2-globulin - nephrotic syndrome 4. a1-globulin flat curve - juvenile cirrhosis (AAT deficiency) 5. Spikes of a1,a2 and ß globulin bands - inflammation

Decrease in serum total protein is seen in what conditions?

(1) Malnutrition / Thiamin deficiency (2) Glomerulonephritis – disorder characterized by an inability of kidney to retain large molecular weight protein (3) Hemorrhage (4) Liver damage

It is a disorder characterized by an inability of kidney to retain large molecular weight protein

Glomerulonephritis

Increase serum total protein is seen in what conditions?

(1) Hemoconcentration (2) Infectious hepatitis

What are the sources of Urinary protein?

Blood Kidney Urine tract Vagina Prostate

Reference range for CSF proteins

15-45 mg/dL

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