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פותח על ידי קלירמאש פתרונות בע"מ -
3‐Oxoecdysteroid reductases in Manduca sexta midgut
Year:
1992
Authors :
סבובודה, ג'יימס
;
.
Volume :
21
Co-Authors:
Weirich, G.F., Insect Neurobiology and Hormone Laboratory, Agricultural Research Service, U.S. Department of Agriculture, Belgtsville, Maryland, United States
Svoboda, J.A., Insect Neurobiology and Hormone Laboratory, Agricultural Research Service, U.S. Department of Agriculture, Belgtsville, Maryland, United States
Facilitators :
From page:
91
To page:
102
(
Total pages:
12
)
Abstract:
The 80,000g supernatant o larval midgut homogenates of the tobacco hornworm, Manduca sexta, was fractionated by affinity chromatography on Blue Sepharose CL‐6B and by anion exchange chromatography on Q Sepharose. Both methods resolved one major 3‐oxoecdysteroid 3α‐reductase and three major 3‐oxoecdysteroid 3β‐reductases. The 3β‐reducates reacted only with BADPH as cosubstrate. The 3α‐reductase was active with both NADPH and NADH, and the NADPH/NADH activity ratio increased with the NaCl concentration (0–0.5 M) in the incubation mixtures. The 3‐α‐reductase and one of the 3‐β‐reductases showed very similar chromatographic properties, and their isoelectric points were 5.2 and 5.8, respectively. © 1992 Wiley‐Liss, Inc. Copyright © 1992 Wiley‐Liss, Inc.
Note:
Related Files :
3α‐hydroxyecdysteroid
3β‐hydroxyecdysteroid
3‐dehydroecdysone
3‐ketosteroid
ketoreductase
עוד תגיות
תוכן קשור
More details
DOI :
10.1002/arch.940210203
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
32168
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 01:07
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Scientific Publication
3‐Oxoecdysteroid reductases in Manduca sexta midgut
21
Weirich, G.F., Insect Neurobiology and Hormone Laboratory, Agricultural Research Service, U.S. Department of Agriculture, Belgtsville, Maryland, United States
Svoboda, J.A., Insect Neurobiology and Hormone Laboratory, Agricultural Research Service, U.S. Department of Agriculture, Belgtsville, Maryland, United States
3‐Oxoecdysteroid reductases in Manduca sexta midgut
The 80,000g supernatant o larval midgut homogenates of the tobacco hornworm, Manduca sexta, was fractionated by affinity chromatography on Blue Sepharose CL‐6B and by anion exchange chromatography on Q Sepharose. Both methods resolved one major 3‐oxoecdysteroid 3α‐reductase and three major 3‐oxoecdysteroid 3β‐reductases. The 3β‐reducates reacted only with BADPH as cosubstrate. The 3α‐reductase was active with both NADPH and NADH, and the NADPH/NADH activity ratio increased with the NaCl concentration (0–0.5 M) in the incubation mixtures. The 3‐α‐reductase and one of the 3‐β‐reductases showed very similar chromatographic properties, and their isoelectric points were 5.2 and 5.8, respectively. © 1992 Wiley‐Liss, Inc. Copyright © 1992 Wiley‐Liss, Inc.
Scientific Publication
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