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אסיף מאגר המחקר החקלאי
פותח על ידי קלירמאש פתרונות בע"מ -
Resistance of soybean vegetative storage proteins (S-VSPs) to proteolysis by rumen microorganisms
Year:
2002
Authors :
בדני, חנה
;
.
גלילי, שמואל
;
.
גנון (גלברט), דנה
;
.
דבש, לבנה
;
.
לנדאו, יאן
;
.
Volume :
50
Co-Authors:
Guenoune, D., Department of Agronomy and Natural Resources, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Landau, S., Department of Agronomy and Natural Resources, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Amir, R., Department of Plant Physiology, Migal Technological Center, Kiryat Shmona 12100, Israel
Badani, H., Department of Agronomy and Natural Resources, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Devash, L., Department of Agronomy and Natural Resources, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Wolf, S., Department of Field Crops, Vegetables and Genetics, Faculty of Agriculture, Hebrew University, Rehovot 76100, Israel
Galili, S., Department of Agronomy and Natural Resources, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Facilitators :
From page:
2256
To page:
2260
(
Total pages:
5
)
Abstract:
Soybean vegetative storage proteins (S-VSPs) are lysine-rich and, hence, are potentially of high nutritive value for high productive ruminants. Using S-VSPs from wild-type soybean and from transgenic tobacco plants expressing either one of the two S-VSPs subunits (S-VSPα or S-VSPβ) or both, we tested their stability in cow rumen fluid under in situ conditions, using SDS-polyacrylamide gel electrophoresis. Proteolysis and degradation pattern of S-VSPs from transgenic tobacco leaves occurred relatively fast compared with that of wild-type (WT) soybean plants. Comparing the two S-VSPs subunits expressed in transgenic plants, we found that S-VSPα was degraded much faster than S-VSPβ. The degradation pattern of S-VSPs in transgenic tobacco plants expressing both subunits resembled that of WT soybean. In contrast, the degradation pattern of transgenic tobacco plants expressing a single subunit was different. These finding suggest that the quaternary structure of S-VSPs may be an important factor determining their resistance to rumen degradation. Our results also suggest that the stability to rumen proteolysis of a given protein, when expressed in a transgenic plant, may not always be predictable and has to be verified.
Note:
Related Files :
Animal
Animals
cattle
Female
gene expression
Genetics
Glycine max
metabolism
nutrition
transgenic plants
עוד תגיות
תוכן קשור
More details
DOI :
10.1021/jf010949k
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
22856
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:54
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Scientific Publication
Resistance of soybean vegetative storage proteins (S-VSPs) to proteolysis by rumen microorganisms
50
Guenoune, D., Department of Agronomy and Natural Resources, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Landau, S., Department of Agronomy and Natural Resources, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Amir, R., Department of Plant Physiology, Migal Technological Center, Kiryat Shmona 12100, Israel
Badani, H., Department of Agronomy and Natural Resources, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Devash, L., Department of Agronomy and Natural Resources, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Wolf, S., Department of Field Crops, Vegetables and Genetics, Faculty of Agriculture, Hebrew University, Rehovot 76100, Israel
Galili, S., Department of Agronomy and Natural Resources, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Resistance of soybean vegetative storage proteins (S-VSPs) to proteolysis by rumen microorganisms
Soybean vegetative storage proteins (S-VSPs) are lysine-rich and, hence, are potentially of high nutritive value for high productive ruminants. Using S-VSPs from wild-type soybean and from transgenic tobacco plants expressing either one of the two S-VSPs subunits (S-VSPα or S-VSPβ) or both, we tested their stability in cow rumen fluid under in situ conditions, using SDS-polyacrylamide gel electrophoresis. Proteolysis and degradation pattern of S-VSPs from transgenic tobacco leaves occurred relatively fast compared with that of wild-type (WT) soybean plants. Comparing the two S-VSPs subunits expressed in transgenic plants, we found that S-VSPα was degraded much faster than S-VSPβ. The degradation pattern of S-VSPs in transgenic tobacco plants expressing both subunits resembled that of WT soybean. In contrast, the degradation pattern of transgenic tobacco plants expressing a single subunit was different. These finding suggest that the quaternary structure of S-VSPs may be an important factor determining their resistance to rumen degradation. Our results also suggest that the stability to rumen proteolysis of a given protein, when expressed in a transgenic plant, may not always be predictable and has to be verified.
Scientific Publication
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