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Á¦¸ñ Purine Nucleoside Phosphorylase Activities in Sera of Leprosy Patients
ÀúÀÚ Mi soon park, Seung Churl Lee, Inn Ki Chun, Young Pio Kim ¼Ò¼Ó Dept. of Dermeatology, Chonam University Medical School Kwangju, Korea
³âµµ 1987 ±Ç 20
È£ 1 ¹øÈ£
½ÃÀÛÆäÀÌÁö 49 ³¡ÆäÀÌÁö 52
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¿ä¾à Purine nucleoside phosphorylase (PNPase) is an enzyme, which catalyses the
conversion of purine nucleotide to the free purine base and found in most human
tissues. A role for PNPase in the immune response has been suggested by the findings
that the enzyme is deficient in the lymphocytes of the patients with normal B-cell
immunity and defective T-cell immunity.
Leprosy is an infectious disease caused by Mycobacterium leprae and divided into two
polar forms.
The present study was designed to measure the activity of PNPase in sera of blood
from patients with lepromatous and tuberculoid leprosy and from normal subjects.
The PNPase activities in sera of normal subjects, tuberculoid leprosy and lepromatous
leprosy were (3.90¡¾1.03)¡¿104 units/L, (3.20¡¾0.76)¡¿104
units/L, (1.87¡¾0.67)¡¿104 units/L respectively.
In the results, the PNPase activities in sera had no difference between normal
subjects and tuberculoid leprosy, but those in leprornatous leprosy were significantly
lowered than normal one.
From the results, it is suggester that the enzyme may partcipate in the cell-mediated
immunity and demonstrated biochemically that lepromatous leprosy is considered to be
manifested in persons with deficient cell mediated immunity.
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