Serum albumin, often referred to simply as albumin, is the most abundant plasma

protein in humans and other mammals. Albumin is essential for maintaining the os
motic pressure needed for proper distribution of body fluids between intravascul
ar compartments and body tissues. It also acts as a plasma carrier by non-specif
ically binding several hydrophobic steroid hormones and as a transport protein f
or hemin and fatty acids. Albumin (when ionized in water at pH 7.4, as found in
the body) is negatively charged. The glomerular basement membrane is also negati
vely charged in the body; some studies suggest that this prevents the filtration
of albumin in the urine. According to this theory, that charge plays a major ro
le in the selective exclusion of albumin from the glomerular filtrate. A defect
in this property results in nephrotic syndrome leading to albumin loss in the ur
ine. Nephrotic syndrome patients are sometimes given albumin to replace the lost
albumin.Because smaller animals (for example rats) function at a lower blood pr
essure, they need less oncotic pressure to balance this, and thus need less albu
min to maintain proper fluid distribution.Serum albumin contains eleven distinct
binding domains for hydrophobic compounds. One hemin and six long-chain fatty a
cids can bind to serum albumin at the same time [1].
Alkaline phosphatase (ALP) is a hydrolase enzyme responsible for removing phosph
ate groups from many types of molecules, including nucleotides, proteins, and al
kaloids. The process of removing the phosphate group is called dephosphorylation
. As the name suggests, alkaline phosphatases are most effective in an alkaline
environment. The optimal pH for the activity of the E. coli enzyme is 8.0[1] whi
le the bovine enzyme optimum pH is slightly higher at 8.5 It is sometimes used s
ynonymously as basic phosphatase. The normal range is 20 to 140 IU/L High ALP le
vels can show that the bile ducts are blocked.[6] Levels are significantly highe
r in children and pregnant women. Also, elevated ALP indicates that there could
be active bone deposition occurring as ALP is a byproduct of osteoblast activity
(such as the case in Paget's disease of bone).Lowered levels of ALP are less co
mmon than elevated levels.
Alanine transaminase or ALT is a transaminase enzyme . It is also called serum g
lutamic pyruvic transaminase (SGPT) or alanine aminotransferase (ALAT).
ALT is found in serum and in various bodily tissues, but is most commonly associ
ated with the liver. It catalyzes the two parts of the alanine cycle.
An amylase is an enzyme that breaks starch down into sugar. Amylase is present i
n human saliva, where it begins the chemical process of digestion. Foods that co
ntain much starch but little sugar, such as rice and potato, taste slightly swee
t as they are chewed because amylase turns some of their starch into sugar in th
e mouth. The pancreas also makes amylase (alpha amylase) to hydrolyse dietary st
arch into di- and trisaccharides which are converted by other enzymes to glucose
to supply the body with energy. Plants and some bacteria also produce amylase.
As diastase, amylase was the first enzyme to be discovered and isolated (by Anse
lme Payen in 1833).[citation needed] Specific amylase proteins are designated by
different Greek letters. All amylases are glycoside hydrolases and act on ?-1,4
-glycosidic bonds. It will start to denature at around 60C. Blood serum amylase
may be measured for purposes of medical diagnosis. A normal concentration is in
the range 21-101 U/L. A higher than normal concentration may reflect one of seve
ral medical conditions, including acute inflammation of the pancreas, macroamyla
semia, perforated peptic ulcer, and mumps. Amylase may be measured in other body
fluids, including urine and peritoneal fluid.
Blood is a specialized bodily fluid that delivers necessary substances to the bo
dy's cells such as nutrients and oxygen and transports waste products away from
those same cells.
Blood Urea Nitrogen (BUN) test is a measure of the amount of nitrogen in the blo
od in the form of urea, and a measurement of renal function. Urea is a substance
secreted by the liver, and removed from the blood by the kidneys.The most commo
n cause of an elevated BUN, azotemia, is poor kidney function, although a serum
creatinine level is a somewhat more specific measure of renal function (see also
renal function).A greatly elevated BUN (>60 mg/dL) generally indicates a modera
te-to-severe degree of renal failure. Impaired renal excretion of urea may be du
e to temporary conditions such as dehydration or shock, or may be due to either
acute or chronic disease of the kidneys themselves.An elevated BUN in the settin
g of a relatively normal creatinine may reflect a physiological response to a re
lative decrease of blood flow to the kidney (as seen in heart failure or dehydra
tion) without indicating any true injury to the kidney. However, an isolated ele
vation of BUN may also reflect excessive formation of urea without any compromis
e to the kidneys.Increased production of urea is seen in cases of moderate or he
avy bleeding in the upper gastrointestinal tract (e.g. from ulcers). The nitroge
nous compounds from the blood are resorbed as they pass through the rest of the
GI tract and then broken down to urea by the liver. Enhanced metabolism of prote
ins will also increase urea production, as may be seen with high protein diets,
steroid use, burns, or fevers.When the ratio of BUN to creatinine (BUN:Cr) is gr
eater than 20, the patient is suspected of having prerenal azotemia. This means
that the pathologic process is unlikely to be due to intrinsic kidney damage.A l
ow BUN usually has little significance, but its causes include liver problems, m
alnutrition (insufficient dietary protein), or excessive alcohol consumption. Ov
erhydration from intravenous fluids can result in a low BUN. Normal changes in r
enal bloodflow during pregnancy will also lower BUN.
lipoprotein is a biochemical assembly that contains both proteins and lipids. Th
e lipids or their derivatives may be covalently or non-covalently bound to the p
roteins. Many enzymes, transporters, structural proteins, antigens, adhesins and
toxins are lipoproteins. Examples include the high density (HDL) and low densit
y (LDL) lipoproteins which enable fats to be carried in the blood stream, the tr
ansmembrane proteins of the mitochondrion and the chloroplast, and bacterial lip
oproteins [1].
Low-density lipoprotein (LDL) is a type of lipoprotein that transports cholester
ol and triglycerides from the liver to peripheral tissues. LDL is one of the fiv
e major groups of lipoproteins; these groups include chylomicrons, very low-dens
ity lipoprotein (VLDL), intermediate-density lipoprotein (IDL), low-density lipo
protein, and high-density lipoprotein (HDL), although some alternative organizat
ional schemes have been proposed. Like all lipoproteins, LDL enables fats and ch
olesterol to move within the water-based solution of the blood stream. LDL also
regulates cholesterol synthesis at these sites. It is used medically as part of
a cholesterol blood test, and since high levels of LDL cholesterol can signal me
dical problems like cardiovascular disease, it is sometimes called bad cholester
ol, (as opposed to HDL, which is frequently referred to as good cholesterol or h
ealthy cholesterol).[1] Because LDLs transport cholesterol to the arteries and c
an be retained there by arterial proteoglycans starting the formation of plaques
, increased levels are associated with atherosclerosis, and thus heart attack, s
troke, and peripheral vascular disease. For this reason, cholesterol inside LDL
lipoproteins is often called bad cholesterol. This is a misnomer. The cholestero
l transported on LDL is the same as cholesterol transported on other lipoprotein
particles. The cholesterol itself is not bad; rather, it is how and where the c
holesterol is being transported, and in what amounts over time, that causes adve
rse effects.
High-density lipoprotein (HDL) is one of the five major groups of lipoproteins (
chylomicrons, VLDL, IDL, LDL, HDL) that enable lipids like cholesterol and trigl
ycerides to be transported within the water-based bloodstream. In healthy indivi
duals, about thirty percent of blood cholesterol is carried by HDL.[1]It is hypo
thesized that HDL can remove cholesterol from atheroma within arteries and trans
port it back to the liver for excretion or re-utilization, which is the main rea
son why HDL-bound cholesterol is sometimes called "good cholesterol", or HDL-C.
A high level of HDL-C seems to protect against cardiovascular diseases, and low
HDL cholesterol levels (less than 40mg/dL or about 1mmol/L) increase the risk for
heart disease.[1] Cholesterol contained in HDL particles is considered benefici
al for the cardiovascular health, in contrast to "bad" LDL cholesterol.
Triglyceride (TG) (more properly known as triacylglycerol ), TAG or triacylglyc
eride) is a glyceride in which the glycerol is esterified with three fatty acids
.[1] It is the main constituent of vegetable oil and animal fats.In the human bo
dy, high levels of triglycerides in the bloodstream have been linked to atherosc
lerosis, and, by extension, the risk of heart disease and stroke. However, the r
elative negative impact of raised levels of triglycerides compared to that of LD
L:HDL ratios is as yet unknown. The risk can be partly accounted for by a strong
inverse relationship between triglyceride level and HDL-cholesterol level.Anoth
er disease caused by high triglycerides is pancreatitis. To lower triglyceride l
evels, one may reduce consumption of fats, alcohol and carbohydrates, particular
ly in rice, and engage in aerobic exercise.
Glucose (Glc), a monosaccharide (or simple sugar) also known as grape sugar, blo
od sugar, or corn sugar, is a very important carbohydrate in biology. The living
cell uses it as a source of energy and metabolic intermediate. Glucose is one o
f the main products of photosynthesis and starts cellular respiration in both pr
okaryotes (bacteria and archaea) and eukaryotes (animals, plants, fungi, and pro
tists).The name "glucose" comes from the Greek word glukus (??????), meaning "sw
eet", and the suffix "-ose," which denotes a sugar.Two stereoisomers of the aldo
hexose sugars are known as glucose, only one of which (D-glucose) is biologicall
y active. This form (D-glucose) is often referred to as dextrose monohydrate, or
, especially in the food industry, simply dextrose (from dextrorotatory glucose[
2]). This article deals with the D-form of glucose. The mirror-image of the mole
cule, L-glucose, cannot be metabolized by cells in the biochemical process known
as glycolysis. proteins. This reaction (glycation) reduces or destroys the func
tion of many enzymes. Scientists can speculate on the reasons why glucose, and n
ot another monosaccharide such as fructose (Fru), is so widely used in organisms
. One reason might be that glucose has a lower tendency, as compared to other he
xose sugars, to non-specifically react with the amino groups of proteins. This r
eaction (glycation) reduces or destroys the function of many enzymes. The low ra
te of glycation is due to glucose's preference for the less reactive cyclic isom
er. Nevertheless, many of the long-term complications of diabetes (e.g., blindne
ss, renal failure, and peripheral neuropathy) are probably due to the glycation
of proteins or lipids. In contrast, enzyme-regulated addition of glucose to prot
eins by glycosylation is often essential to their function.
Creatine kinase (CK), also known as creatine phosphokinase (CPK) or phospho-crea
tine kinase (and sometimes wrongfully as creatinine kinase), is an enzyme (EC 2.
7.3.2) expressed by various tissues and cell types. CK catalyses the conversion
of creatine and consumes adenosine triphosphate (ATP) to create phosphocreatine
and adenosine diphosphate (ADP). This CK enzyme reaction is reversible, such tha
t also ATP can be generated from PCr and ADP.In tissues and cells that consume A
TP rapidly, especially skeletal muscle, but also brain, photoreceptor cells of t
he retina, hair cells of the inner ear, spermatozoa and smooth muscle, phosphocr
eatine serves as an energy reservoir for the rapid buffering and regeneration of
ATP in situ, as well as for intracellular energy transport by the phosphocreati
ne shuttle or circuit.[2] Thus creatine kinase is an important enzyme in such ti
ssues.Clinically, creatine kinase is assayed in blood tests as a marker of myoca
rdial infarction (heart attack), rhabdomyolysis (severe muscle breakdown), muscu
lar dystrophy, and in acute renal failure.
Uric acid (or urate) is an organic compound of carbon, nitrogen, oxygen, and hyd
rogen with the formula C5H4N4O3.
High uric acid
Gout
Excess serum accumulation of uric acid can lead to a type of arthritis known as
gout.Elevated serum uric acid (hyperuricemia) can result from high intake of pur
ine-rich foods, high fructose intake (regardless of fructose's low glycemic inde
x (GI) value) and/or impaired excretion by the kidneys. Saturation levels of uri
c acid in blood may result in one form of kidney stones when the urate crystalli
zes in the kidney. These uric acid stones are radiolucent and so do not appear o
n an abdominal plain x-ray or CT scan. Their presence must be diagnosed by ultra
sound for this reason. Very large stones may be detected on x-ray by their displ
acement of the surrounding kidney tissues. Some patients with gout eventually ge
t uric kidney stones.Gout can occur where serum uric acid levels are as low as 6
mg/dL (~357mol/L), but an individual can have serum values as high as 9.6 mg/dL
(~565mol/L) and not have gout.[18]
Lesch-Nyhan syndrome
Lesch-Nyhan syndrome, an extremely rare inherited disorder, is also associated w
ith very high serum uric acid levels.Spasticity, involuntary movement and cognit
ive retardation as well as manifestations of gout are seen in cases of this synd
rome.
Cardiovascular disease
Although uric acid can act as an antioxidant, excess serum accumulation is often
associated with cardiovascular disease. It is not known whether this is causati
ve (e.g., by acting as a prooxidant ) or a protective reaction taking advantage
of urate's antioxidant properties.
Diabetes
The association of high serum uric acid with insulin resistance has been known s
ince the early part of the 20th century, nevertheless, recognition of high serum
uric acid as a risk factor for diabetes has been a matter of debate. In fact, h
yperuricemia has always been presumed to be a consequence of insulin resistance
rather than its precursor. However, it was shown in a prospective follow-up stud
y that high serum uric acid is associated with higher risk of type 2 diabetes in
dependent of obesity, dyslipidemia, and hypertension.
Metabolic syndrome
Hyperuricemia is associated with components of metabolic syndrome and it has bee
n debated for a while to be a component of it. It has been shown in a recent stu
dy that fructose-induced hyperuricemia may play a pathogenic role in the metabol
ic syndrome. This agrees with the increased consumption of fructose-base drinks
in recent decades and the epidemic of diabetes and obesity.
Uric acid stone formation
Uric acid stones, which form in the absence of secondary causes such as chronic
diarrhea, vigorous exercise, dehydration, and animal protein loading, are felt t
o be secondary to obesity and insulin resistance seen in metabolic syndrome. Inc
reased dietary acid leads to increased endogenous acid production in the liver a
nd muscles which in turn leads to an increased acid load to the kidneys. This lo
ad is handled more poorly because of renal fat infiltration and insulin resistan
ce which are felt to impair ammonia excretion (a buffer). The urine is therefore
quite acidic and uric acid becomes insoluble, crystallizes and stones form. In
addition, naturally present promotor and inhibitor factors may be affected. This
explains the high prevalence of uric stones and unusually acidic urine seen in
patients with type 2 diabetes. Uric acid crystals can also promote the formation
of calcium oxalate stones, acting as "seed crystals" (heterogeneous nucleation)
Low uric acid
Multiple sclerosis
Lower serum values of uric acid have been associated with Multiple Sclerosis. Mu
ltiple sclerosis (MS) patients have been found to have serum levels ~194mol/L, wi
th patients in relapse averaging ~160mol/L and patients in remission averaging ~2
30mol/L. Serum uric acid in healthy controls was ~290mol/L. Conversion factor: 1 m
g/dL=59.48 mol/L
A 1998 study completed a statistical analysis of 20 million patient records, com
paring serum uric acid values in patients with gout and patients with multiple s
clerosis. Almost no overlap between the groups was found.
Uric acid has been successfully used in the treatment and prevention of the anim
al (murine) model of MS. A 2006 study found that elevation of serum uric acid va
lues in multiple sclerosis patients, by oral supplementation with inosine, resul
ted in lower relapse rates, and no adverse effects.
Oxidative stress
Uric acid may be a marker of oxidative stress,and may have a potential therapeut
ic role as an antioxidant.On the other hand, like other strong reducing substanc
es such as ascorbate, uric acid can also act as a prooxidant, particularly at el
evated levels. Thus, it is unclear whether elevated levels of uric acid in disea
ses associated with oxidative stress such as stroke and atherosclerosis are a pr
otective response or a primary cause.
For example, some researchers propose that hyperuricemia-induced oxidative stres
s is a cause of metabolic syndrome. On the other hand, plasma uric acid levels c
orrelate with longevity in primates and other mammals.This is presumably a funct
ion of urate's antioxidant properties.
Sources of uric acid
In many instances, people have elevated uric acid levels for hereditary reasons.
Diet may also be a factor; eating large amounts of sea salt can cause increased
levels of uric acid.(Medical consultation is recommended before using large qua
ntities of sea salt in daily cooking.
Purines are found in high amounts in animal internal organ food products, such a
s liver.A moderate amount of purine is also contained in beef, pork, poultry, fi
sh and seafood, asparagus, cauliflower, spinach, mushrooms, green peas, lentils,
dried peas, beans, oatmeal, wheat bran and wheat germ.
Examples of high purine sources include: sweetbreads, anchovies, sardines, liver
, beef kidneys, brains, meat extracts (e.g., Oxo, Bovril), herring, mackerel, sc
allops, game meats, and gravy.
Moderate intake of purine-containing food is not associated with an increased ri
sk of gout.
Serum uric acid can be elevated due to high fructose intake, reduced excretion b
y the kidneys, and or high intake of dietary purine.
Added fructose can be found in processed foods and soda beverages as sucrose, or
in some countries, as high fructose corn syrup.
Causes of low uric acid
Low uric acid (hypouricemia) can have numerous causes.Low dietary zinc intakes c
ause lower uric acid levels. This effect can be even more pronounced in women ta
king oral contraceptive medication.Sevelamer, a drug indicated for prevention of
hyperphosphataemia in patients with chronic renal failure, can significantly re
duce serum uric acid.
Urea or carbamide is an organic compound with the chemical formula (NH2)2CO. The
molecule has two amine (-NH2) residues joined by a carbonyl (-CO-) functional g
roup.
Urea plays an important role in the metabolism of nitrogen-containing compounds
by animals, and is the main nitrogen-containing substance in the urine of mammal
s. Being solid, colourless, odorless, neither acidic nor alkaline, highly solubl
e in water, and relatively non-toxic, urea is widely used in fertilizers as a co
nvenient source of nitrogen. Urea is also an important raw material for the chem
ical industry. The synthesis of this organic compound by Friedrich Whler in 1828
from an inorganic precursor was an important milestone in the development of che
mistry.
The terms urea and carbamide are also used for a class of chemical compounds sha
ring the same functional group RR'N-CO-NRR', namely a carbonyl group flanked by
two organic amine residues. Example include carbamide peroxide, allantoin, and h
ydantoin. Ureas are closely related to biurets and related in structure to amide
s, carbamates, diimides, carbodiimides, and thiocarbamides.
Urea is synthesized in the body of many organisms as part of the urea cycle, eit
her from the oxidation of amino acids or from ammonia. In this cycle, amino grou
ps donated by ammonia and L-aspartate are converted to urea, while L-ornithine,
citrulline, L-argininosuccinate, and L-arginine act as intermediates. Urea produ
ction occurs in the liver and is regulated by N-acetylglutamate. Urea is found d
issolved in blood (in the reference range of 2.5 to 7.5 mmol/liter) and is excre
ted by the kidney as a component of urine. In addition, a small amount of urea i
s excreted (along with sodium chloride and water) in sweat.


The same information, shown in molarity rather than mass.
Aminoacids from ingested food which are not used for the synthesis of proteins a
nd other biological substances are oxidized by the body, yielding urea and carbo
n dioxide, as an alternative source of energy.[3] The oxidation pathway starts w
ith the removal of the amino group by a transaminase, the amino group is then fe
d into the urea cycle.
Ammonia (NH3) is another common byproduct of the metabolism of nitrogenous compo
unds. Ammonia molecules are smaller, more volatile and more mobile than urea's.
If allowed to accumulate, ammonia would raise the pH in cells to toxic levels. T
herefore many organisms convert ammonia to urea, even though this synthesis has
a net energy cost. Being practically neutral and highly soluble in water, urea i
s a safe vehicle for the body to transport and excrete excess nitrogen.
In humans
The handling of urea by the kidneys is a vital part of human metabolism. Besides
its role as carrier of waste nitrogen, urea also plays a role in the countercur
rent exchange system of the nephrons, that allows for reabsorption of water and
critical ions from the excreted urine. Urea is reabsorbed in the inner medullary
collecting ducts of the nephrons,[4] thus raising the osmolarity in the medulla
ry interstitium surrounding the thin ascending limb of the loop of Henle, which
in turn causes water to be reabsorbed. By action of the urea transporter 2, some
of this reabsorbed urea will eventually flow back into the thin ascending limb
of the tubule, through the collecting ducts, and into the excreted urine.
This mechanism, which is controlled by the antidiuretic hormone, allows the body
to create hyperosmotic urine, that has a higher concentration of dissolved subs
tances than the blood plasma. This mechanism is important to prevent the loss of
water, to maintain blood pressure, and to maintain a suitable concentration of
sodium ions in the blood plasma.