1.

Blood pH
The acidity or alkalinity of blood. The pH of any fluid is the measure of the hydrogen

ion (H-) concentration. A pH of 7 is neutral. The lower the pH, the more acidic the blood.
A variety of factors affect blood pH including what is ingested, vomiting, diarrhea, lung
function, endocrine function, kidney function, and urinary tract infection. The normal
blood pH is tightly regulated between 7.35 and 7.45.
2.

Base Deficit
2 to +2 mEq/liter

B.E.

Other sources:

normal

reference range is between -5

to +3.
The base excess indicates the amount of excess or insufficient level of
bicarbonate in the system.

(A negative base excess indicates a base

deficit in the blood.) A negative base excess is equivalent to an acid

excess. A value outside of the normal range (-2 to +2 mEq) suggests a
metabolic cause for the abnormality.

Calculated value.

The base excess

is defined as the amount of H+ ions that would be required to return the

pH of the blood to 7.35 if the pCO2 were adjusted to normal.
It can be estimated by the equation:
Base excess = 0.93 (HCO3 - 24.4 + 14.8(pH - 7.4))
Alternatively: Base excess = 0.93HCO3 + 13.77pH - 124.58
A base excess > +3 = metabolic alkalosis a base excess < -3 = metabolic
acidosis

3.

Myoglobin Urine

a.

Definition
Urine myoglobin is a test to detect the presence of myoglobin in a sample of urine.

Myoglobin is a protein in heart and skeletal muscles. When a muscle is exercised, it uses
up available oxygen. Myoglobin has oxygen attached to it, which provides extra oxygen
for the muscle to keep up a high level of activity for a longer period of time.
When muscle is damaged, the myoglobin in muscle cells is released into the bloodstream.
The kidneys help remove myoglobin out of the body. In large amounts, myoglobin can
damage the kidneys.
b. How the Test is Performed
A clean-catch (midstream) urine sample is needed.
Men or boys should first wipe clean the head of the penis. Women or girls need to wash
the area between the lips of the vagina with soapy water and rinse well.
As you start to urinate, allow a small amount to fall into the toilet bowl (this clears the
urethra of contaminants). Then, in a clean container, catch about 1 to 2 ounces of urine
and remove the container from the urine stream. Give the container to the health care
provider or assistant.
In infants, thoroughly wash the area where urine exits the body. Open a urine collection
bag (a plastic bag with an adhesive paper on one end), and place it on your infant. For
boys, place the entire penis in the bag and attach the adhesive to the skin. For girls, place
the bag over the labia. Diaper as usual over the secured bag.
This procedure may take a couple of attempts -- lively infants can move the bag, causing
the urine to be absorbed by the diaper. Check the infant frequently and change the bag
after the infant has urinated into it. Drain the urine from the bag into the container
provided by your health care provider.
Deliver it to the laboratory or your health care provider as soon as possible upon
completion.
c.

How the Test Will Feel

The test involves only normal urination, which should cause no discomfort.
d. Why the Test is Performed
Urine myoglobin levels may be taken if your health care provider thinks you have muscle
damage, including skeletal and heart muscle damage. It may also be done if you have
acute kidney failure without an obvious cause.
e.

Normal Results

A normal urine sample does not have myoglobin. Sometimes a normal result is reported
as negative.
Normal value ranges may vary slightly among different laboratories. Talk to your doctor
about the meaning of your specific test results.
f.

What Abnormal Results Mean

Abnormal results may be due to:

4.

Heart attack

Malignant hyperthermia(very rare)

Muscular dystrophy

Rhabdomyolysis

Skeletal muscle inflammation (myositis)

Skeletal muscle ischemia (oxygen deficiency)

Skeletal muscle trauma

Cola-colored Urine

Rhabdomyolysis.
This refers to the breakdown of striated muscle fibres and the release of potentially toxic

muscle enzymes, myoglobin and intracellular constituents such as potassium and calcium
into the systemic circulation. Biochemically it is defined as an acute increase of
creatinine kinase to more than five times the upper normal limit where the fraction of
CK-MB is <5% (thereby excluding an MI).
Referred to as the hidden killer with a mortality of 5%, the consequences of
rhabdomyolysis can be fatal due to hypovolaemia, hyperkalaemia, metabolic acidosis,
acute renal failure and disseminated intravascular coagulation (DIC) that ultimately
results from the intracellular damage caused by abnormal circulation of intracellular
contents and the subsequent activation of calcium dependent proteases and lipases.
Unfortunately, its presentation is often very non-specific and its incidence is therefore
underestimated. The most common presenting symptoms however are myalgia and cocacola coloured urine, which is caused by myoglobinuria (myoglobin >250ng/ml, which
corresponds with >100mg of muscle breakdown). This presents with a urine positive
dipstick for haem (blood) but without red cells on urine microscopy.
5.

Potassium plasma
The normal range for serum potassium is narrow (3.5 to 5.5 mEq/L), and minor

departure from this range (by less than 1.0 mEq/L) is associated with significant
morbidity and mortality. Although a 1.0 mEq change in concentration is small in absolute
terms, it changes the KI:Ke ratio by 25%. Therefore rapid evaluation and, when indicated,
treatment of hypo- and hyperkalemia are critical. Table summarizes the clinical
consequence of hypo- and hyperkalemia. These symptoms, signs, and laboratory findings
should alert the clinician to the possible existence of a significant derangement in serum
potassium. Neuromuscular and cardiac signs and symptoms can be quite similar and can
include nonspecific minor complaints (e.g., weakness, tiredness, and palpitation), as well
as major symptoms (paralysis and sudden death). As indicated in table, hypokalemia can
also present with gastrointestinal, metabolic, and renal abnormalities.
Hypokalemia
Neuromuscular
Cardiac

Weakness
Paralysis
Arrhythmia

Hyperkalemia
Weakness
Paralysis
Arrhythmia

6.

ECG: U wave
Gastrointestinal Ileus
Metabolic
Hyperglycemia
NH3 production
Renal
Polyuria
Creatine kinase serum

ECG: peaked T wave

NH3 production

Reference Range, Interpretation, Collection and Panels

Description
CK, formerly known as creatinine phosphokinase, is an important protein enzyme
catalyzing the reversible phosphorylation reaction.
ADP + creatine phosphate ATP + creatine
CK is a dimeric molecule composed of M and/or B subunits. Two protein subunits form
into 3 different isozymes: CK-MM, CK-MB, and CK-BB. CK-MM and CK-BB are
abundantly found in skeletal muscle and the brain, respectively. CK-MB is found
predominantly in the myocardium (making up 15-30% of the CK in the heart muscle),
while a much smaller proportion is found in the skeletal muscle (making up only 5-7% of
the CK in the skeletal muscle). As CK is found in the inner mitochondrial membrane and
cytoplasm, it can be released into the blood through cell membrane disruption and death.
CK-MB is sensitive and specific to myocardial injury. CK-MB begins to rise 4-6 hours
after the onset of acute myocardial injury and returns to baseline level after 36-48
hours.Thus, CK-MB is also a useful marker of reinfarction or infarct extension. However,
a small percentage of B-subunit can be found in skeletal muscle. Thus, muscle
breakdown can also increase the both total CK and CK-MB level.
The normal value for CK-MB is 3-5% of total CK, but peak CK-MB level can range from
15-30% of total CK in post-myocardial infarction. Therefore, percentage criteria were
proposed to distinguish between skeletal muscle and myocardial damage. However, these
criteria were found to have decreased sensitivity for acute myocardial infarction in
trauma patients and decreased specificity in patients with chronic skeletal muscle

abnormalities. Therefore, the measurement of troponin is recommended in these patients.

CK is degraded by proteolysis either locally or in lymph nodes. Hypothyroidism can
retard this CK degradation.[15]
Indications/Applications
Because the greatest amount of CK is found in skeletal muscle, CK is a useful marker of
skeletal muscle breakdown. Therefore, CK is most commonly used for diagnosis and
monitoring among patients with neuromuscular disorders including the following:
Inflammatory myopathies such as polymyositis, dermatomyositis
Infectious myopathies
Dystrophinopathies such as Duchenne and Becker muscular dystrophy
Rhabdomyolysis
Drugs-induced myopathies resulting from statins, fibrates, colchicines, antimalarials, and
cocaine
Neuroleptic malignant syndrome
Malignant hyperthermia
Endocrine myopathies such as hypothyroidism
Periodic paralyses
CK-MB is found mostly in myocardium. Therefore, CK-MB is a useful marker for acute
myocardial injury. CK-MB can be elevated in the following:
Acute myocardial infarction
Myocarditis

Cardiac trauma or contusion

Cardiac surgery
Endomyocardial biopsy
Defibrillation or cardioversion
As stated in the 2004 American College of Cardiology/American Heart Association
(ACC/AHA) guidelines, serial measurement of CK-MB can be useful in indicating the
success of reperfusion after fibrinolysis in conjunction with clinical variables. Because
CK-MB has a short half-life and returns to baseline level within 48 hours after acute
myocardial infarction, CK-MB can be used as a marker for reinfarction in conjunction
with clinical chest pain and EKG changes after 18 hours from the onset of a myocardial
infarction.
Moreover, studies have demonstrated a relationship between CK-MB level and clinical
outcome among patients with acute coronary syndromes. Specifically, increased CK-MB
is related to higher mortality after both non-ST and ST elevation myocardial infarction.
Furthermore, serial sampling CK-MB can be used to estimate the infarct size by
formulating time activity curves and using mathematic model of the amount depleted
from the myocardium. However, this is not routinely done because multiple blood
samples are required to avoid the likelihood of missing the peak enzyme concentration.
Moreover, CK-MB can underestimate infarct size in a large doughnut infarct pattern
because reduced blood flow limits CK-MB efflux.
Considerations
CK is a useful test for diagnosing and monitoring of neuromuscular diseases. Because
CK can rise in any condition causing muscle injury, considering this possibility is
important to prevent misdiagnosis in the following circumstances:
Recent strenuous exercise

Repeated intramuscular injection or needle electromyography (EMG)

Recent trauma with muscle injury
Epileptic seizure or severe dystonia
High fever accompanied by shivering
Systemic disorders such as viral infection, connective tissue disorder, celiac disease, renal
failure, or critically ill patients
CK-MB is found almost exclusively in myocardium. It is widely used as a marker for
acute myocardial infarction. However, 5-7% of CK-MB is found in skeletal muscle.
Thus, skeletal muscle injury can also cause elevated CK-MB, which can lead to
misinterpretation. Note that other noncoronary conditions that can cause elevated CK-MB
level include asthma, renal failure, pulmonary embolism, muscle disease, and
hypothyroidism.
Despite less sensitivity and specificity for acute myocardial infarction compared to
troponin, CK-MB is still a useful cardiac marker. CK-MB rises and returns to baseline
more rapidly, which make it a preferred marker for reinfarction. Moreover, CK-MB can
be used to indicate successful reperfusion after fibrinolysis, to estimate the infarct size,
and to predict infarct-related mortality. In addition, elevated CK-MB level post
percutaneous coronary intervention is associated with increased mortality at 3-4 months.