Identification of Two Plastid Proteins in the Dinoflagellate <i>Alexandrium affine</i> That Are Substantially Down-Regulated by Nitrogen-Depletion by Fred Wang-Fat Lee (2339839)

“…Five of these nine spots were all identified as isoforms of the plastid Form II ribulose-1,5 bisphosphate carboxylase/oxygenase (Rubisco II), while an additional four protein spots with a molecular weight of 50 kDa were identified as isoforms of a novel protein named nitrogen-associated protein 50 (NAP50). …”

Identification of Two Plastid Proteins in the Dinoflagellate <i>Alexandrium affine</i> That Are Substantially Down-Regulated by Nitrogen-Depletion by Fred Wang-Fat Lee (2339839)

“…Five of these nine spots were all identified as isoforms of the plastid Form II ribulose-1,5 bisphosphate carboxylase/oxygenase (Rubisco II), while an additional four protein spots with a molecular weight of 50 kDa were identified as isoforms of a novel protein named nitrogen-associated protein 50 (NAP50). …”

Identification of Two Plastid Proteins in the Dinoflagellate <i>Alexandrium affine</i> That Are Substantially Down-Regulated by Nitrogen-Depletion by Fred Wang-Fat Lee (2339839)

“…Five of these nine spots were all identified as isoforms of the plastid Form II ribulose-1,5 bisphosphate carboxylase/oxygenase (Rubisco II), while an additional four protein spots with a molecular weight of 50 kDa were identified as isoforms of a novel protein named nitrogen-associated protein 50 (NAP50). …”

Identification of Two Plastid Proteins in the Dinoflagellate <i>Alexandrium affine</i> That Are Substantially Down-Regulated by Nitrogen-Depletion by Fred Wang-Fat Lee (2339839)

“…Five of these nine spots were all identified as isoforms of the plastid Form II ribulose-1,5 bisphosphate carboxylase/oxygenase (Rubisco II), while an additional four protein spots with a molecular weight of 50 kDa were identified as isoforms of a novel protein named nitrogen-associated protein 50 (NAP50). …”

Identification of Two Plastid Proteins in the Dinoflagellate <i>Alexandrium affine</i> That Are Substantially Down-Regulated by Nitrogen-Depletion by Fred Wang-Fat Lee (2339839)

“…Five of these nine spots were all identified as isoforms of the plastid Form II ribulose-1,5 bisphosphate carboxylase/oxygenase (Rubisco II), while an additional four protein spots with a molecular weight of 50 kDa were identified as isoforms of a novel protein named nitrogen-associated protein 50 (NAP50). …”

Identification of Two Plastid Proteins in the Dinoflagellate <i>Alexandrium affine</i> That Are Substantially Down-Regulated by Nitrogen-Depletion by Fred Wang-Fat Lee (2339839)

“…Five of these nine spots were all identified as isoforms of the plastid Form II ribulose-1,5 bisphosphate carboxylase/oxygenase (Rubisco II), while an additional four protein spots with a molecular weight of 50 kDa were identified as isoforms of a novel protein named nitrogen-associated protein 50 (NAP50). …”

Identification of Two Plastid Proteins in the Dinoflagellate <i>Alexandrium affine</i> That Are Substantially Down-Regulated by Nitrogen-Depletion by Fred Wang-Fat Lee (2339839)

“…Five of these nine spots were all identified as isoforms of the plastid Form II ribulose-1,5 bisphosphate carboxylase/oxygenase (Rubisco II), while an additional four protein spots with a molecular weight of 50 kDa were identified as isoforms of a novel protein named nitrogen-associated protein 50 (NAP50). …”

Identification of Two Plastid Proteins in the Dinoflagellate <i>Alexandrium affine</i> That Are Substantially Down-Regulated by Nitrogen-Depletion by Fred Wang-Fat Lee (2339839)

“…Five of these nine spots were all identified as isoforms of the plastid Form II ribulose-1,5 bisphosphate carboxylase/oxygenase (Rubisco II), while an additional four protein spots with a molecular weight of 50 kDa were identified as isoforms of a novel protein named nitrogen-associated protein 50 (NAP50). …”

Identification of Two Plastid Proteins in the Dinoflagellate <i>Alexandrium affine</i> That Are Substantially Down-Regulated by Nitrogen-Depletion by Fred Wang-Fat Lee (2339839)

“…Five of these nine spots were all identified as isoforms of the plastid Form II ribulose-1,5 bisphosphate carboxylase/oxygenase (Rubisco II), while an additional four protein spots with a molecular weight of 50 kDa were identified as isoforms of a novel protein named nitrogen-associated protein 50 (NAP50). …”

Identification of Two Plastid Proteins in the Dinoflagellate <i>Alexandrium affine</i> That Are Substantially Down-Regulated by Nitrogen-Depletion by Fred Wang-Fat Lee (2339839)

“…Five of these nine spots were all identified as isoforms of the plastid Form II ribulose-1,5 bisphosphate carboxylase/oxygenase (Rubisco II), while an additional four protein spots with a molecular weight of 50 kDa were identified as isoforms of a novel protein named nitrogen-associated protein 50 (NAP50). …”

Identification of Two Plastid Proteins in the Dinoflagellate <i>Alexandrium affine</i> That Are Substantially Down-Regulated by Nitrogen-Depletion by Fred Wang-Fat Lee (2339839)

“…Five of these nine spots were all identified as isoforms of the plastid Form II ribulose-1,5 bisphosphate carboxylase/oxygenase (Rubisco II), while an additional four protein spots with a molecular weight of 50 kDa were identified as isoforms of a novel protein named nitrogen-associated protein 50 (NAP50). …”

Tandem Imaging of Breath Ethanol and Acetaldehyde Based on Multiwavelength Enzymatic Biofluorometry by Kenta Iitani (4175995)

“…The oxidation of EtOH by ADH_OX in the presence of NAD⁺ produced NADH, which was subsequently oxidized by diaphorase (DP) with resazurin, leading to the resorufin formation, characterized by red fluorescence (excitation at 560 nm and fluorescence at 590 nm). Reduction of AcH by ADH_RD consumed NADH, leading to a decrease in blue fluorescence (ex. 340 nm, fl. 490 nm). …”

Tandem Imaging of Breath Ethanol and Acetaldehyde Based on Multiwavelength Enzymatic Biofluorometry by Kenta Iitani (4175995)

“…The oxidation of EtOH by ADH_OX in the presence of NAD⁺ produced NADH, which was subsequently oxidized by diaphorase (DP) with resazurin, leading to the resorufin formation, characterized by red fluorescence (excitation at 560 nm and fluorescence at 590 nm). Reduction of AcH by ADH_RD consumed NADH, leading to a decrease in blue fluorescence (ex. 340 nm, fl. 490 nm). …”

Tandem Imaging of Breath Ethanol and Acetaldehyde Based on Multiwavelength Enzymatic Biofluorometry by Kenta Iitani (4175995)

“…The oxidation of EtOH by ADH_OX in the presence of NAD⁺ produced NADH, which was subsequently oxidized by diaphorase (DP) with resazurin, leading to the resorufin formation, characterized by red fluorescence (excitation at 560 nm and fluorescence at 590 nm). Reduction of AcH by ADH_RD consumed NADH, leading to a decrease in blue fluorescence (ex. 340 nm, fl. 490 nm). …”

Tandem Imaging of Breath Ethanol and Acetaldehyde Based on Multiwavelength Enzymatic Biofluorometry by Kenta Iitani (4175995)

“…The oxidation of EtOH by ADH_OX in the presence of NAD⁺ produced NADH, which was subsequently oxidized by diaphorase (DP) with resazurin, leading to the resorufin formation, characterized by red fluorescence (excitation at 560 nm and fluorescence at 590 nm). Reduction of AcH by ADH_RD consumed NADH, leading to a decrease in blue fluorescence (ex. 340 nm, fl. 490 nm). …”

Tandem Imaging of Breath Ethanol and Acetaldehyde Based on Multiwavelength Enzymatic Biofluorometry by Kenta Iitani (4175995)

“…The oxidation of EtOH by ADH_OX in the presence of NAD⁺ produced NADH, which was subsequently oxidized by diaphorase (DP) with resazurin, leading to the resorufin formation, characterized by red fluorescence (excitation at 560 nm and fluorescence at 590 nm). Reduction of AcH by ADH_RD consumed NADH, leading to a decrease in blue fluorescence (ex. 340 nm, fl. 490 nm). …”

Tandem Imaging of Breath Ethanol and Acetaldehyde Based on Multiwavelength Enzymatic Biofluorometry by Kenta Iitani (4175995)

“…The oxidation of EtOH by ADH_OX in the presence of NAD⁺ produced NADH, which was subsequently oxidized by diaphorase (DP) with resazurin, leading to the resorufin formation, characterized by red fluorescence (excitation at 560 nm and fluorescence at 590 nm). Reduction of AcH by ADH_RD consumed NADH, leading to a decrease in blue fluorescence (ex. 340 nm, fl. 490 nm). …”

Tandem Imaging of Breath Ethanol and Acetaldehyde Based on Multiwavelength Enzymatic Biofluorometry by Kenta Iitani (4175995)

“…The oxidation of EtOH by ADH_OX in the presence of NAD⁺ produced NADH, which was subsequently oxidized by diaphorase (DP) with resazurin, leading to the resorufin formation, characterized by red fluorescence (excitation at 560 nm and fluorescence at 590 nm). Reduction of AcH by ADH_RD consumed NADH, leading to a decrease in blue fluorescence (ex. 340 nm, fl. 490 nm). …”

Tandem Imaging of Breath Ethanol and Acetaldehyde Based on Multiwavelength Enzymatic Biofluorometry by Kenta Iitani (4175995)

“…The oxidation of EtOH by ADH_OX in the presence of NAD⁺ produced NADH, which was subsequently oxidized by diaphorase (DP) with resazurin, leading to the resorufin formation, characterized by red fluorescence (excitation at 560 nm and fluorescence at 590 nm). Reduction of AcH by ADH_RD consumed NADH, leading to a decrease in blue fluorescence (ex. 340 nm, fl. 490 nm). …”

Tandem Imaging of Breath Ethanol and Acetaldehyde Based on Multiwavelength Enzymatic Biofluorometry by Kenta Iitani (4175995)

“…The oxidation of EtOH by ADH_OX in the presence of NAD⁺ produced NADH, which was subsequently oxidized by diaphorase (DP) with resazurin, leading to the resorufin formation, characterized by red fluorescence (excitation at 560 nm and fluorescence at 590 nm). Reduction of AcH by ADH_RD consumed NADH, leading to a decrease in blue fluorescence (ex. 340 nm, fl. 490 nm). …”