Cysteine pI= 5 buffer= 8 favors? migrate?

The application of electrophoresis in medicine and diagnosis of illness, knowing that your proteins in the body are composed of amino acids. It may be used for diagnostic purposes

happens when the hemoglobin is different in terms of shape (crescent shape) instead of a biconcave disk where it would have a tendency of lower oxygen-carrying capacity and it may clog causing thrombosis.

The difference of a normal hemoglobin and a sickle cell sequence of protein is one only which lies on the _ amino acid where on Hb-A (normal) has glutamic acid in the case of hemoglobin with sickle cell disease, there is a mutation that occurred wherein it has the same sequence on the first five of proteins. On the _ position, instead of glutamic acid, it became VALINE

For the person with sickle cell trait (carrier), they have 2 _ where they have the normal and sickle cell hemoglobin. However, the patient does not manifest the symptoms of the disease as they are still a carrier but there is a likelihood that the person may pass it to its offspring.

Glutamic acid pi= 3.22 Valine pI=5.92. The normal hemoglobin, glutamic acid at 3.22 in electrophoresis medium buffered at 4, will exist as a _ charge and will migrate towards the _. However, in sickle trait, valine buffered at 4, it will exist as _ charged amino acid and will migrate towards the _ electrode.

major storage of glucose in the liver

lysis means

beginning of creating glucose from new substances

naubos na ang glycogen

in gluconeogenesis, carbohydrate is not anymore the source of glucose but

source of energy is protein

infections of kwashiorkor

migration of solvent from low concentration of solute going to higher region of solute

antibodies are called immunoglobulines globulins are antibodies kwashiorkor has no protein = no antibodies

process of separating mixtures of amino acid based on their isoelectric point

glycine

alanine

valine

leucine

isoleucine

• it is used in the synthesis of collagen. • fast acting energy source. • natural moisturizing factor

it is used in the synthesis of phospholipids (phospholipids usually found on cell membrane double lipid layer made of phospo serine is precursor)

it is involved in porphyrin metabolism (nakikita sa rbc particulary form as heme sa hemoglobin non protein component)

is the most common aromatic amino acid and is useful in synthesis of amines (amine kasama ang dopamine, epinephrine, norephinephrine, even melanin. Melanin come from tyrosine a precursor before we convert it needs enzyme tyrosinase)

it is a precursor for the synthesis of neurotransmitters and hormones and biological pigment melanin

the least frequently used aromatic amino acid (serotonin 5-hydroxytryptophan as well as niacin vit b3 galing den sa tryp)

it helps in the initiation of protein synthesis (has sulfur needs to produce dna methylation kasama sa process ng nucleus to produce protein synthesized with )

cysteine

asparagine

Glutamine

located mostly at TCA

it is the only amino acid that can pass trough the blood brain barrier

helps in the absorption of calcium and important in the formation of collagen, bones and connective tissues

arginine

histidine

it is a structural analog of cysteine wherein the sulfur is replaced by selenium. • it is located in the active sites of enzymes which participates in redox reaction

it is produced by a specific trna and aminoacyl trna synthetase (wala sa human bacteria specifically archae or archaeans nakatira sa extreme environments some are methanogens produces methane aa their waste product)

Proteinogenic Amino Acids:

Non-Proteinogenic Amino Acids:

non proteogenic AA

Peptide bond formation

A peptide bond can be represented as two resonance isomers. Peptide bond has a partial double bond characteristics. A peptide bond has two kinds of spatial configuration. has two possible orientation cyst and trans

the chain is already more than 10 amino acid in the sequence, we now call it polypeptide.

Components of peptide bond: • Residues: Amino acids in the peptide; denotes what is left after the release of H2O when an amino acid forms a peptide link upon joining the peptide chain. • N Terminal Amino Acid: Amino acid residue at the end with a free α-amino group • C Terminal Amino Acid: Amino acid with a free –COO- group Nomenclature: • Each amino acid beginning from the N terminal end has the –ine (or –ic acid) replaced by –yl • The last amino acid at the C terminal end of the peptide has its full name.

Many relatively small peptides are biochemically active that functions as: except

Many peptides are being used medicinally and are recognized for being highly selective and efficacious and, at the same time, relatively safe and well tolerated • Cyclosporine - immunosuppresant • Desmopressin - synthetic vasopressin • Leuprorelin (LupronTM) - prostrate cancer • Lantus ® - DM • Exenatide (Byetta ®) - type II diabetes • Enfuvirtide (Fuzeon ®) - HIV fusion inhibitor

Catabolism is the breakdown anabolism is the synthesis or build-up When we are talking about amino acid catabolism and anabolism, the major organ responsible is the liver.

Protein turnover

Protein turnober mechanism

Nitrogen metabolism has two phase reaction

The backbone of amino acid are amino group, central carbon, and carboxyl group. When amino group is removed, carbon will remain forming carbon skeleton.

Nitrogen leaves the body as urea, ammonia, & other products derived from amino acid metabolism _ the only form of inorganic nitrogen which can be utilized by living cells. It is toxic in the body so it has to be converted to urea which is excreted via the urine.

Intestinal Absorption – appears to be active, energy requiring process. L- isomer are absorbed more rapidly than D-isomer, dicarboxylic and diamino are absorbed slowly than neutral amino acid

negative nitrogen balance

nitrogen balance

positive nitrogen balance

deamination

Catalyzes the pyridine nucleotide-linked reversible deamination of L-Glutamic Acid. Either NAD or NADP is used as the coenzyme

• Carbamyl Phophate Synthetase – catalyzes the ATP dependent formation of carbamyl phosphate • Carbamyl Phosphate is the initial reactant in the formation of both Urea and Pyrimidines

SYNTHETHASE AND SYNTHASE ➢Synthetase involves ATP and bond formation ➢Synthase involves bond breakage and may or may not involve ATP

Catalyzes the synthesis of glutamine Plasma glutamine synthesized largely by the liver, accounts for some 20-25% of the total plasma amino acid nitrogen

Synthesized in animal tissues by pathway analogous to glutamine synthetase

Amino group is transferred from 1 molecule to another w/o intermediate formation of ammonia

Most active and widely distributed transaminases are those which involves L- Glutamate and a- ketoglutarate

• Provide reversible link between carbohydrates and amino acid metabolism • Oxidative deamination of amino acid • Involved directly in the biosynthesis of a number of A.A • Degradation of many A.A involves the initial removal of the amino group by transamination

• Urea – is the predominant nitrogen end product from amino group derived from A.A. • Ammonia – 2/3 portion of urinary ammonia is formed in the kidney by the enzymatic hydrolysis of blood glutamine, the remainder being produced by the oxidative deamination of blood A.A. • Uric Acid – principal end product of purine metabolism • Creatine – is the end product of the metabolism of arginine, glycine, and methionine • Prior to excretion, creatine phosphate is converted to creatinine • Normal adult excretes 0.37 to 0.67 creatinine/day

Ammonia is toxic that's why the liver needs to convert ammonia to urea which could be excreted through the urine. If uric acid builds up in the body, the disease associated with it is gouty arthritis. Before the formation of gout, level of uric acid will rise which is called hyperuricemia. Uric acid is not the principal byproduct of protein metabolism, but purine. Purine and pyrimidine are nitrogenous bases of the DNA.

Ketogenic

Glucogenic

Ketogenesis also known as lipid synthesis. Pyruvate commonly seen as pyruvic acid which came from transamination reaction. Alanine is a precursor of sugar.

glucogenic : essential

Glucogenic and ketogenic : non essential

ketogenic

which more severe

SOME HUMAN GENETIC DISORDERS AFFECTING AMINO ACID METABOLISM Albinism

Homogentisate 1,2-dioxygenase

Argininosuccinate lyase

Cystathionine B-synthase

MAPLE SYRUP URINE DISEASE

Phenylketonuria

HYPERVALINEMIA

Storage and/or release of cystine from lysosomes

Renal and intestinal transport of cysteine

Renal transport of neutral A.A

Histidemia

Isovaleric acidemia

• A disorder of amino acid metabolism that results in a congenital hypopigmentation of ocular and systemic tissues • Mutations interfere with the enzyme tyrosinase (tyrosine 3- monooxygenase). Enzyme synthesizes melanin from the amino acid tyrosine

X-LINKED OCULAR ALBINISM

OCULOCUTANEUOUS ALBINISM [OCA]

• Common in Puerto Rico • Similar to OCA but bowel, heart, kidney, and lung diseases or bleeding disorders, such as hemophilia and more likely, too

• Rare form caused by mutation in the CHS1/LYST genes • Symptoms similar to OCA but hair can appear silvery and skin slightly gray • There may be defects in the WBC, making infections common

There is no treatment to albinism as the problem lies on the genes or it is a genetic anomaly. Symptomatic relief or treatment is done. They are very prone to skin cancer and their eyes can be easily damaged by the sunlight. They can have surgery if needed. If there is problem in blood, the blood disorder is treated but basically, it's symptomatic.

Cystinosis

• Malfunctioning kidneys and corneal crystals • If intermediate cystinosis is left untreated, complete kidney failure will occur, but usually not until the late teens to mid-twenties

Caused by lack of the enzyme (phenylalanine hydroxylase) needed to convert phenylalanine to tyrosine • This disorder causes buildup of phenylalanine, which is toxic to the brain • Symptoms include intellectual disability, seizures, nausea, vomiting, and must body ofor