חיפוש מתקדם
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
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.
פותח על ידי קלירמאש פתרונות בע"מ -
הספר "אוצר וולקני"
אודות
תנאי שימוש
Resistance of soybean vegetative storage proteins (S-VSPs) to proteolysis by rumen microorganisms
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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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