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ENZYME RESEARCH: STUDIES FROM NATIONAL ACADEMY OF SCIENCE ADD NEW FINDINGS IN THE AREA OF ENZYME RESEARCH
Pharma Law Weekly
October 21, 2008
Scientists discuss in 'Complex of dipeptidyl peptidase II with
adenosine deaminase' new findings in enzyme research. According
to recent research from Yerevan, Armenia, "Dipeptidyl peptidase
II (DPPII) from bovine kidney cortex and lung was purified to the
electrophoretically homogeneous state. The molecular and catalytic
characteristics of the enzyme were determined."
"It was revealed that DPPII preparations possess adenosine deaminase
(ADA) activity at all purification steps. For the first time, the
ADA-binding ability of DPPII has been shown similar to the well-known
ADA-binding enzyme, DPPIV. The dissociation constant of the DPPII-ADA
complex was estimated using a resonant mirror biosensor (80 nM),
fluorescence polarization (60 nM), and differential spectroscopy
(36 nM) techniques," wrote S.G. Sharoyan and colleagues, National
Academy of Science (see also Enzyme Research).
The researchers concluded: "The data demonstrate that DPPII can form a
complex with ADA, but with one order of magnitude higher dissociation
constant than that of DPPIV (7.8 nM)."
Sharoyan and colleagues published their study in Biochemistry (Complex
of dipeptidyl peptidase II with adenosine deaminase. Biochemistry,
2008;73(8):943-9).
For additional information, contact S.G. Sharoyan, Buniatyan Institute
of Biochemistry, Armenian National Academy of Sciences, Yerevan,
Armenia.
Publisher contact information for the journal Biochemistry is: Maik
Nauka, Interperiodica, C, O Kluwer Academic-Plenum Publishers, 233
Spring St., New York, NY 10013-1578, USA.
From: Emil Lazarian | Ararat NewsPress
Pharma Law Weekly
October 21, 2008
Scientists discuss in 'Complex of dipeptidyl peptidase II with
adenosine deaminase' new findings in enzyme research. According
to recent research from Yerevan, Armenia, "Dipeptidyl peptidase
II (DPPII) from bovine kidney cortex and lung was purified to the
electrophoretically homogeneous state. The molecular and catalytic
characteristics of the enzyme were determined."
"It was revealed that DPPII preparations possess adenosine deaminase
(ADA) activity at all purification steps. For the first time, the
ADA-binding ability of DPPII has been shown similar to the well-known
ADA-binding enzyme, DPPIV. The dissociation constant of the DPPII-ADA
complex was estimated using a resonant mirror biosensor (80 nM),
fluorescence polarization (60 nM), and differential spectroscopy
(36 nM) techniques," wrote S.G. Sharoyan and colleagues, National
Academy of Science (see also Enzyme Research).
The researchers concluded: "The data demonstrate that DPPII can form a
complex with ADA, but with one order of magnitude higher dissociation
constant than that of DPPIV (7.8 nM)."
Sharoyan and colleagues published their study in Biochemistry (Complex
of dipeptidyl peptidase II with adenosine deaminase. Biochemistry,
2008;73(8):943-9).
For additional information, contact S.G. Sharoyan, Buniatyan Institute
of Biochemistry, Armenian National Academy of Sciences, Yerevan,
Armenia.
Publisher contact information for the journal Biochemistry is: Maik
Nauka, Interperiodica, C, O Kluwer Academic-Plenum Publishers, 233
Spring St., New York, NY 10013-1578, USA.
From: Emil Lazarian | Ararat NewsPress