Genetic diversity assessment of a set of introduced mung bean accessions (Vigna radiata L.)
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چکیده
منابع مشابه
Mung Bean (Vigna radiata) Seedlings'
Two forms of Fd-NADP+ oxidoreductase (FNR) isoproteins have been purified and characterized from the first foliage leaves of 5d-old mung bean (Vigna radiata). They could be separated by either Mono Q HR 515 or ferredoxin (Fd)-Sepharose 48 affinity columns. Based on immunoblot analysis and N-terminal amino acid sequences, one form resembles the FNR purified from photosynthetic tissues of higher ...
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BACKGROUND: Vermicompost in sustainable agriculture is very useful for improving soil porosity and thereby providing more nutrients to crop. OBJECTIVES: Current research was conducted to evaluate effect of biofertilizer (vermicompost) under different level of irrigation on crop production and protein yield. METHODS: This study was c...
متن کاملBiosynthesis of Phosphatidylglycerol in Isolated Mitochondria of Etiolated Mung Bean (Vigna radiata L.) Seedlings.
Phosphatidylglycerophosphate synthase (sn-glycerol-3-phosphate:CDP-diacylglycerol phosphatidyltransferase) and phosphatidylglycerophosphate phosphatase were characterized in mung bean (Vigna radiata L.) mitochondria. The synthase has a rather broad pH optimum between 7 and 9, whereas the phosphatase has one of about 7. Both enzymic activities are stimulated by Triton X-100 and require divalent ...
متن کاملPurification and characterization of lipoxygenase from mung bean (Vigna radiata L.) germinating seedlings
This study reports purification and characterization of lipoxygenase protein from mung bean germinating seedlings. Lipoxygenases (LOXs) are key enzymes in seed germination. The purified mung bean LOX has resolved into two peaks by chromatofocusing, one has highest LOX activity with an isoelectric point of 5.84 and the other has lowest LOX activity with an isoelectric point of 5.52. The purified...
متن کاملPurification and regulatory properties of mung bean (vigna radiata L.) serine hydroxymethyltransferase.
Serine hydroxymethyltransferase, the first enzyme in the pathway for interconversion of C(1) fragments, was purified to homogeneity for the first time from any plant source. The enzyme from 72-h mung bean (Vigna radiata L.) seedlings was isolated using Blue Sepharose CL-6B and folate-AH-Sepharose-4B affinity matrices and had the highest specific activity (1.33 micromoles of HCHO formed per minu...
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ژورنال
عنوان ژورنال: The Crop Journal
سال: 2018
ISSN: 2214-5141
DOI: 10.1016/j.cj.2017.08.004