Screening of genetically enhanced cotton varieties with a high content of protein markers, proteinase inhibitors, was carried out for the first time. It was found that only 5 of 68 studied cotton selection lines were resistant to wilt, black root rot, and gummosis.
Crambe kotschyanaBoiss. and C. orientalis L. (Cruciferae) are herbaceous perennial feed plants that are endemic and broadly distributed in Uzbekistan [1]. Young shoots of the plants are used in food. Dried roots are processed into flour. The starch content in roots is almost the same as in potatoes. The green plant is consumed by several animals (camels and sheep). The nutritional value of C. kotschyana exceeds that of many currently cultivated plants, especially the contents of essential amino acids and macroscopic and trace elements [2]. Alkaloids were first found by us in these plant species [3]. The S-containing alkaloids goitrin and goitridin [4] in addition to the known compound N-(benzimidazolyl-2)-O-ethylcarbamate [5] were previously isolated from the CHCl 3 -soluble total alkaloids in the EtOH extract of the aerial part and roots of two Crambe species.In continuation of this research, the alkaline aqueous solution remaining after extraction of total alkaloids from C. kotschyana and C. orientalis, which showed a reaction for N-containing compounds, was investigated for amino-acid content. Several plant species are known to accumulate free amino acids characteristic of this species. Individual nitrogenexchange steps and plant food values are commonly studied by determining free and bound amino acids.Therefore, we isolated and determined quantitatively the protein content in the alkaline aqueous solution remaining after extraction of total alkaloids. It contained 10% protein [6].Free and bound amino acids were determined quantitatively on a T339 amino-acid analyzer. Free amino acids were isolated by heating a weighed portion (100 mg) of protein in distilled H 2 O (10 mL) on a water bath for 5 min. The extract was evaporated in a rotary evaporator and prepared for analysis on the amino-acid analyzer [7]. Bound amino acids were determined after acid hydrolysis in HCl (5.7 N) for 24 h at 110°C in vacuo [8]. Table 1 presents the analytical amino-acid composition. Table 1 shows that the amino acids were found mainly in the bound state. The total amino acids made up 2.12% whereas the total bound amino acids made up 16.9%. All essential amino acids, i.e., valine, threonine, isoleucine, leucine, lysine, phenylalanine, histidine, and arginine, which are not synthesized in vivo and are assimilated from food, were found in the amino-acid composition of Crambe protein. Glutamine, leucine, glycine, alanine, arginine, and lysine dominated the free and bound amino acids.HPLC was used to determine the molecular weights (MWs) of the isolated proteins. The MWs were determined by constructing a calibration curve using the logarithm of the protein MWs as a function of their retention times. The MW of the protein (peptide) was 10 kDa.The observed hypoglycemic effect of the C. kotschyana proteins was interesting. We studied the effect of the protein component mainly in untreated animals. The investigations showed that blood sugar was reduced by 14% (at the most effective dose of 50 mg/kg) 3 h after a single administration of the...
A bifunctional inhibitor of proteinase and α-amylase from local varieties of corn kernels was isolated and characterized. Its amylolytic and proteolytic inhibiting activities in high-lysine local varieties of corn were determined.
The inhibitory activities of the new gossypol-free cotton variety Bukhara-9 and varieties UzFA-705 and Mirishkor were compared. It was found that Bukhara-9 and UzFA-705 had the same inhibitory activity as the resistant regionalized variety An-Bayaut-2. The inhibitory activity of Mirishkor was greater than that of variety Turon, which was developed for growing in arid zones. It was shown that Mirishkor proteinase inhibitors suppressed practically fully growth in vitro of the phytopathogenic fungus Fusarium oxysporum.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
customersupport@researchsolutions.com
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.