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changes in substrate(s) and product
changes in substrate(s) and products(s) in the reaction mixture. Continuous methods (change in absorbance, fluorescence, or
pH) are very much preferred over methods that require taking aliquots at selected times, stopping the reaction by inactivating the
enzyme, and adding one or more reagents to form a measurable derivative of either the substrate or product (preferable).
Since an enzyme is highly specific for only one or a few substrates, it follows that it is relatively easy to measure that enzyme
selectively even among hundreds of other enzymes of different specificities. The enzyme activity can be used to determine not
only the presence of an enzyme (qualitative), but also how much enzyme is present (quantitative), based on its rate under
controlled conditions.
Some substrates and products do not differ greatly in physical and/or chemical properties; therefore it is difficult to determine the
first-order rate constant,
k
1 (Eq. 7). In these cases, coupled enzyme assays should be considered, where the product, P1, of the
first enzyme is a substrate of an added second enzyme. The product, P2, of the second enzyme is then chosen for measurement
(Eq. 7). In order to measure
k
1 correctly, the relation
k
2[E2]
@
100
k
1[E1] should be used.
pH) are very much preferred over methods that require taking aliquots at selected times, stopping the reaction by inactivating the
enzyme, and adding one or more reagents to form a measurable derivative of either the substrate or product (preferable).
Since an enzyme is highly specific for only one or a few substrates, it follows that it is relatively easy to measure that enzyme
selectively even among hundreds of other enzymes of different specificities. The enzyme activity can be used to determine not
only the presence of an enzyme (qualitative), but also how much enzyme is present (quantitative), based on its rate under
controlled conditions.
Some substrates and products do not differ greatly in physical and/or chemical properties; therefore it is difficult to determine the
first-order rate constant,
k
1 (Eq. 7). In these cases, coupled enzyme assays should be considered, where the product, P1, of the
first enzyme is a substrate of an added second enzyme. The product, P2, of the second enzyme is then chosen for measurement
(Eq. 7). In order to measure
k
1 correctly, the relation
k
2[E2]
@
100
k
1[E1] should be used.
0/5000
changes in substrate(s) and products(s) in the reaction mixture. Continuous methods (change in absorbance, fluorescence, or
pH) are very much preferred over methods that require taking aliquots at selected times, stopping the reaction by inactivating the
enzyme, and adding one or more reagents to form a measurable derivative of either the substrate or product (preferable).
Since an enzyme is highly specific for only one or a few substrates, it follows that it is relatively easy to measure that enzyme
selectively even among hundreds of other enzymes of different specificities. The enzyme activity can be used to determine not
only the presence of an enzyme (qualitative), but also how much enzyme is present (quantitative), based on its rate under
controlled conditions.
Some substrates and products do not differ greatly in physical and/or chemical properties; therefore it is difficult to determine the
first-order rate constant,
k
1 (Eq. 7). In these cases, coupled enzyme assays should be considered, where the product, P1, of the
first enzyme is a substrate of an added second enzyme. The product, P2, of the second enzyme is then chosen for measurement
(Eq. 7). In order to measure
k
1 correctly, the relation
k
2[E2]
@
100
k
1[E1] should be used.
pH) are very much preferred over methods that require taking aliquots at selected times, stopping the reaction by inactivating the
enzyme, and adding one or more reagents to form a measurable derivative of either the substrate or product (preferable).
Since an enzyme is highly specific for only one or a few substrates, it follows that it is relatively easy to measure that enzyme
selectively even among hundreds of other enzymes of different specificities. The enzyme activity can be used to determine not
only the presence of an enzyme (qualitative), but also how much enzyme is present (quantitative), based on its rate under
controlled conditions.
Some substrates and products do not differ greatly in physical and/or chemical properties; therefore it is difficult to determine the
first-order rate constant,
k
1 (Eq. 7). In these cases, coupled enzyme assays should be considered, where the product, P1, of the
first enzyme is a substrate of an added second enzyme. The product, P2, of the second enzyme is then chosen for measurement
(Eq. 7). In order to measure
k
1 correctly, the relation
k
2[E2]
@
100
k
1[E1] should be used.
Sedang diterjemahkan, harap tunggu..
perubahan substrat (s) dan produk (s) dalam campuran reaksi. Metode kontinyu (perubahan absorbansi, fluoresensi, atau
pH) sangat banyak disukai daripada metode yang memerlukan mengambil aliquot pada waktu yang dipilih, menghentikan reaksi dengan menonaktifkan yang
enzim, dan menambahkan satu atau lebih pereaksi untuk membentuk turunan terukur baik substrat atau produk (lebih).
Karena enzim sangat spesifik untuk hanya satu atau beberapa substrat, berarti itu relatif mudah untuk mengukur enzim yang
selektif bahkan di antara ratusan enzim lain kekhususan yang berbeda. Aktivitas enzim dapat digunakan untuk menentukan tidak
hanya kehadiran enzim (kualitatif), tetapi juga berapa banyak enzim hadir (kuantitatif), berdasarkan tingkat di bawah
kondisi yang terkendali.
Beberapa substrat dan produk tidak berbeda jauh secara fisik dan / atau sifat kimia; oleh karena itu sulit untuk menentukan
tingkat orde pertama konstan,
k
1 (Persamaan. 7). Dalam kasus ini, tes enzim ditambah harus dipertimbangkan, di mana produk, P1, dari
enzim pertama adalah substrat enzim kedua ditambahkan. Produk, P2, enzim kedua kemudian dipilih untuk pengukuran
(Persamaan. 7). Untuk mengukur
k
1 benar, hubungan
k
2 [E2]
@
100
k
1 [E1] harus digunakan.
pH) sangat banyak disukai daripada metode yang memerlukan mengambil aliquot pada waktu yang dipilih, menghentikan reaksi dengan menonaktifkan yang
enzim, dan menambahkan satu atau lebih pereaksi untuk membentuk turunan terukur baik substrat atau produk (lebih).
Karena enzim sangat spesifik untuk hanya satu atau beberapa substrat, berarti itu relatif mudah untuk mengukur enzim yang
selektif bahkan di antara ratusan enzim lain kekhususan yang berbeda. Aktivitas enzim dapat digunakan untuk menentukan tidak
hanya kehadiran enzim (kualitatif), tetapi juga berapa banyak enzim hadir (kuantitatif), berdasarkan tingkat di bawah
kondisi yang terkendali.
Beberapa substrat dan produk tidak berbeda jauh secara fisik dan / atau sifat kimia; oleh karena itu sulit untuk menentukan
tingkat orde pertama konstan,
k
1 (Persamaan. 7). Dalam kasus ini, tes enzim ditambah harus dipertimbangkan, di mana produk, P1, dari
enzim pertama adalah substrat enzim kedua ditambahkan. Produk, P2, enzim kedua kemudian dipilih untuk pengukuran
(Persamaan. 7). Untuk mengukur
k
1 benar, hubungan
k
2 [E2]
@
100
k
1 [E1] harus digunakan.
Sedang diterjemahkan, harap tunggu..
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