MYOGLOBIN:
It is a oxygen binding and storing
protein. Its low molecular weight and cytoplasmic location accounts for its
early release following muscle (heart or skeletal) injury. It cannot be used in
differential diagnosis of muscle injury or cardiac injury.
Measured in serum by RIA, latex
agglutination, and immunoassay based on monoclonal antibodies
LACTATE DEHYDROGENASE (EC 1.1.1.27) ISOENZYMES:
It is a cytoplasmic enzyme. This
enzyme has mol weight of 134,000 and has four peptides chain of two types: M
for muscle (or A) and H for heart (or B) each under separate genetic control as
like M and B of CK. LD is inhibited by both pyruvate and lactate in excess
although the effect of pyruvate is greater. Oxidation of –SH in enzyme and its
inactivation is prevented by cysteine or glutathione.
Highest activities are found in
skeletal muscle, liver, heart, kidney, and red blood cells.
Isoenzymes % of LDH activity (Source)
q LDH-1 (H4)
Mostly
heart 60%, RBC 40%, kidney 28%
q LDH-2 (H3M) Mostly kidney, myocardium, RBC,
30-34%
q LDH-3 (H2M2) Mostly spleen, lung, kidney, RBC
q LDH-4 (HM3) Mostly
Spleen, Lung, RBC, Kidney
q LDH-5 (M4) Mostly liver 94%, skeletal
muscle 76%
A different sixth LD isoenzyme LD-X
(also called LDc) composed of four X (or C) subunits is present in
post pubertal human testes. A seventh LD, called LD-6 has been identified in
the sera of severely ill patients.
LDH catalyzes the reversible
conversion of pyruvate to lactate.
(Source: Tietz Clinical Chemistry, 4th Edition) |
Analytical Measurement:
Enzymatic
measurement:
(Source: Tietz Clinical Chemistry, 4th Edition) |
The decrease in absorbance at 340
nm followed. At pH 8.8 to 9.8 the reversible reaction is favored.
Reference range : 125-220 IU/L
Isoenzyme analysis –
It can be done by electrophoresis or
immunoinhibition assay where antibodies inhibit other isoenzymes except LD1.
Formation of NBT formazan is the detection technique after electrophoretic
separation.
(Source: Harper's Illustrated biochemistry, 28th Edition) |
No comments:
Post a Comment