The Enzyme activity can be affected by factors

 

The aim of this introduction is to give an insight
into enzymes. The enzyme that will be studied during this experiment is
alkaline phosphatase. An enzyme assay will be developed for this enzyme. Calf
and bovine ALP assay will be used in the lab. During validation in house ALP
assay will be compared to commercially available human AlP assay using spiked
QC samples.

In every plant and animal enzymes are found. They are
protein- based substances. No plant, animal or human can live without enzymes.
It is a vital part of existence. Thousands of enzymes have been identified in
the human body. These enzymes are constantly changing and renewing. Chemical
reactions are started by enzymes, also speed up reactions. Substrates are
molecules that enzymes act upon. Enzymes then convert the substrate into
different molecules known as products. Enzyme catalysis is needed in order for
metabolic processes to occur at fast enough rate. There are known to be over
five thousand biochemical reactions that enzymes catalyze.

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Enzyme
problems are associated with many medical conditions. For example, a deficiency
of the digestive enzyme lactase, which breaks down milk sugar can lead to
lactose intolerance. Inherited disorders can also cause enzyme defects that may
cause extreme consequences. For example, children born with Tay-Sachs disease
have a genetic abnormality with an enzyme called beta-hexosaminidase A. The
impaired function of this single enzyme leads to destruction of nerve cells in
the brain and spinal cord. Children born with this disorder usually die in
early childhood.

 

Enzymes
in relation to chemical properties are like any catalyst and are not consumed
in chemical reactions. They also do not alter the equilibrium of a reaction.
Although enzymes differ from other catalysts as they are more specific. Enzyme
activity can be affected by factors such as inhibitors which are
molecules that decrease enzyme activity. Activators are molecules
that increase activity. Enzyme inhibitors include therapeutic drugs and
poisons.

An
enzyme’s activity can also be affected by factors such as temperature and PH.
Enzymes are proteins. Proteins can denature when subjected to high level of
heat, salt concentrations, mechanical forces, organic solvents and concentrated
acid or base solutions. Temperature usually increases reaction rate, but when a
certain temperature is reached the reaction rate can decrease. When pH is
increased or decreased the different acid and amine groups on side chain is
altered. This results in overall change to structure and shape of the enzyme.

Enzyme
inhibitors are an important part of the body as they can block an enzymes
activity. They can kill a pathogen or correct metabolic imbalances. There are
three types of inhibitors competitive, non-competitive and substrate
inhibition. Competitive inhibition involves any compound which closely resembles
the chemical structure and molecular type of the structure. The inhibitor and
the substrate molecule both compete for the same active site. The inhibitor
sticks to the enzyme and prevents any substrate molecules from reaction with
the enzyme. An example of this is methanol poisoning. Non- competitive
inhibitor is a substance that interacts with the enzyme but usually not at the
active site. The non-competitive effect is to change the shape of the enzyme
and also the active site. This results in the substrate no longer being able to
react with the enzyme to give a reaction. Penicillin works by inhibiting a
bacterial enzyme that is responsible for forming cross-links in bacteria cell
walls. This stops reproduction. Substrate inhibition occurs with about twenty
per cent of all known enzymes. Substrate inhibition occurs when two molecules
of substrate can bind to the enzyme and this then blocks activity.

Enzymes
have many roles in the body such as food digestion. Food must be broken down
into nutrients to be absorbed and used by the body. Digestive system enzymes
belong to a class of enzymes called hydrolases. These enzymes cause a reaction
called hydrolysis. This reaction breaks down large molecules into smaller
units. There are many different types of enzymes to break down different food
components. An example of this is pepsin and trypsin which digest dietary
proteins.

Cells
contain genetic material called chromosomes, each chromosome carries an array
of genes that encode individual genetics. This genetic material is in the form
of a molecule called deoxyribonucleic acid, DNA. When cells in your body
divide, each newly created cell must contain an exact copy of your DNA. To
carry out this replication the body relies on specific enzymes. For example,
enzymes called helicases and gyrases unwind the tightly coiled DNA strands so
they can be copied. DNA polymerase enzymes participate in the actual copying
process. DNA ligase enzymes are involved in finalizing the copying process.

 

Phosphatases area type of enzymes that catalyse the removal of
phosphate groups by hydrolysis of phosphate ester bonds. Phosphatases act in
opposite manner to kinases and are important in the body with relation to metabolism
and cell signaling. Alkaline phosphates are the phosphatase that will be examined during this
project. Alkaline phosphatase enzymes are found in eukaryotes and prokaryotes. It
is also active in many other tissues, particularly in the liver and kidneys. The
intestine, liver and kidney and placenta are all organs in which AP is especially
present. However, AP is also expressed in blood cells such as neutrophils and
vascular cells like endothelial cells. This results in the enzyme being active
everywhere in the human body. Alkaline phosphatase is also present in bone
tissue and plays a vital role in the formation of bone material. AP helps to
breakdown proteins in the body and comes in different forms. The highest concentration
found in liver, bone and . Alkaline phosphates are a hydrolase enzyme responsible
for removing phosphate groups from many types of molecules including nucleotides,
proteins and alkaloids. This process is known as dephosphorylating. Alkaline phosphatase
is best suited to an alkaline environment.

 

 

Alkaline
phosphatase exists in multiple forms and the forms are found in different
organs possess distinct properties. Human ALPs can be classified into different
tissue-specific forms according to the specificity of the tissue. Such as
placental alkaline phosphatase, intestinal alkaline phosphatase,
liver/bone/kidney alkaline phosphatase and germ cell alkaline phosphatase.

Alkaline
phosphatase is a very important enzyme in relation to human health. An alkaline
phosphatase level test measures the amount of alkaline phosphatase enzyme in
the body’s bloodstream. The test is often a routine part of other blood tests
and requires a blood sample drawn by needle from a vein in the arm.  Normal range is 40-130 units per liter. The
required amount can vary with age and gender. High levels of ALP are normally
seen in children undergoing growth spurts and in pregnant women.  Abnormal levels of ALP can cause problems. An
ALP test can detect such problems as liver disease or bone disease. High levels
of ALP are a result of liver disease, gall bladder disease or bone disease.
Liver disease like hepatitis can increase ALP in the body. Liver cells release
higher levels of ALP when ducts are blocked or a tumor is present. High levels
when cancers spread into bone such as leukemia. Lower levels of ALP at an
amount lower than 40 units per liter results in decreased levels of alp. Patients
with malnutrition and intestinal diseases like celiac or scurvy has decreased
levels of ALP. Methods of measuring ALP incude an enzyme assay and quantitative
colorimetric method.

 

Enzyme
assays are laboratory method of measuring enzymatic activity and monitoring
protein enzyme protein while its being purified. When assaying enzymes factors
such as temperature, pH and ionic strength are all important in order for the
assay to run correctly.