Seed reserve-protein glycosylation in an in vitro preparation from developing cotyledons of Phaseolus vulgaris

Planta ◽  
1979 ◽  
Vol 146 (4) ◽  
pp. 513-520 ◽  
Author(s):  
H. Maelor Davies ◽  
Deborah P. Delmer
Author(s):  
Yan Yu ◽  
Dajun Liu ◽  
Chang Liu ◽  
Zhishan Yan ◽  
Xiaoxu Yang ◽  
...  

2017 ◽  
Vol 42 (2) ◽  
pp. e12485
Author(s):  
Usha Rani Telikicherla ◽  
Mahadeva Naika ◽  
Anilakumar Kandangath Raghavan ◽  
Sashikala Vadakkoot Balakrishnan

2016 ◽  
Vol 42 (4) ◽  
pp. 360-362
Author(s):  
Evelynne Urzêdo Leão ◽  
◽  
Júlio Cesar da Silva ◽  
Fabíola Rodrigues Medeiros ◽  
Gabriela Silva Santa Rosa Macêdo ◽  
...  

RESUMO O feijoeiro-comum (Phaseolus vulgaris) é uma cultura de grande relevância na alimentação da população brasileira. A murcha-de-curtobacterium ou murcha bacteriana, causada por Curtobacterium flaccumfaciens pv. flaccumfaciens (Cff). é uma doença vascular que acomete o feijoeiro causando danos significativos. Neste contexto, o objetivo deste trabalho foi avaliar a ação in vitro de Bacillus spp. na inibição de dois isolados de Cff, colonização do sistema radicular e desenvolvimento de plântulas de feijoeiro-comum. Foram realizados dois ensaios in vitro para verificar a atividade antagônica dos isolados Bacillus licheniformis, B. subtilis e B. subtilis + B. lichenformis a dois isolados de Cff. Todos os isolados de Bacillus spp. apresentaram inibição no crescimento dos isolados de Cff. Não foi observada a colonização das raízes das plântulas de feijoeiro-comum, pelos isolados bacterianos avaliados.


Antioxidants ◽  
2020 ◽  
Vol 9 (12) ◽  
pp. 1181
Author(s):  
Federica Finetti ◽  
Marco Biagi ◽  
Jasmine Ercoli ◽  
Giulia Macrì ◽  
Elisabetta Miraldi ◽  
...  

Phaseolus vulgaris L. (common bean) is a leguminous species that is an important dietary component due to its high content of proteins, unsaturated fatty acids, minerals, dietary fibers and vitamins. Due to the high content of polyphenols, several biological activities have been described for bean extracts, making it possible to include P. vulgaris among food with beneficial effects for human health. Moreover, more than 40,000 varieties of beans have been recognised with different nutraceutical properties, pointing out the importance of food biodiversity. In this work, we describe for the first time the chemical composition and biological activity of a newly recognized Italian variety of P. vulgaris grown in a restricted area of the Tuscany region and named “Fagiola di Venanzio”. Fagiola di Venanzio water extract is rich in proteins, sugars and polyphenols and displays antioxidant, anti-inflammatory and antiproliferative activities in in vitro assays on colon cancer cellular models. Our data indicate that this variety of P. vulgaris appears to be a promising source of bioactive compounds and encourage more in-depth studies to better elucidate the implications of its consumption for public health.


1977 ◽  
Vol 89 (1) ◽  
pp. 235-238 ◽  
Author(s):  
P. E. Russell ◽  
A. E. A. Mussa

SummaryTwo systemic fungicides, benomyl and thiabendazole, were more active than the non-systemic fungicide Drazoxolon in inhibiting fungal growth in vitro. A similar pattern was obtained in glasshouse trials with benomyl and thiabendazole giving adequate protection at low concentrations while Drazoxolon was ineffective unless applied at 50% the commercial product concentration. A field trial using thiabendazole, Drazoxolon and a mixture of benomyl and thiram confirmed the glasshouse results.Some phytotoxicity was noticed with high concentrations of both benomyl and thiabendazole, but satisfactory disease control was achieved using fungicide concentrations which did not induce phytotoxicity.


2017 ◽  
Author(s):  
Jennifer A. Schoborg ◽  
Jasmine Hershewe ◽  
Jessica C. Stark ◽  
Weston Kightlinger ◽  
James E. Kath ◽  
...  

AbstractProtein glycosylation, or the attachment of sugar moieties (glycans) to proteins, is important for protein stability, activity, and immunogenicity. However, understanding the roles and regulations of site-specific glycosylation events remains a significant challenge due to several technological limitations. These limitations include a lack of available tools for biochemical characterization of enzymes involved in glycosylation. A particular challenge is the synthesis of oligosaccharyltransferases (OSTs), which catalyze the attachment of glycans to specific amino acid residues in target proteins. The difficulty arises from the fact that canonical OSTs are large (>70 kDa) and possess multiple transmembrane helices, making them difficult to overexpress in living cells. Here, we address this challenge by establishing a bacterial cell-free protein synthesis platform that enables rapid production of a variety of OSTs in their active conformations. Specifically, by using lipid nanodiscs as cellular membrane mimics, we obtained yields of up to 440 µg/mL for the single-subunit OST enzyme, ‘Protein glycosylation B’ (PglB) from Campylobacter jejuni, as well as for three additional PglB homologs from Campylobacter coli, Campylobacter lari, and Desulfovibrio gigas. Importantly, all of these enzymes catalyzed N-glycosylation reactions in vitro with no purification or processing needed. Furthermore, we demonstrate the ability of cell-free synthesized OSTs to glycosylate multiple target proteins with varying N-glycosylation acceptor sequons. We anticipate that this broadly applicable production method will advance glycoengineering efforts by enabling preparative expression of membrane-embedded OSTs from all kingdoms of life.


Development ◽  
1980 ◽  
Vol 58 (1) ◽  
pp. 195-208
Author(s):  
Irma Thesleff ◽  
Robert M. Pratt

Tunicamycin (TM), an antibiotic that selectively inhibits dolichol-mediated protein glycosylation, inhibited morphogenesis and differentiation of odontoblasts in the molar tooth germ in vitro. These effects of TM are reversible and dose-dependent, and in advanced teeth the effect of TM was not complete unless the basement membrane was removed prior to culture. TM did not prevent secretion of predentin or enamel when added to the cultures after initiation of predentin secretion. TM dramatically inhibited protein glycosylation and the accumulation of labeled proteoglycans and glycoproteins in the basement membrane. Our previous studies indicated that odontoblast differentiation is triggered by an interaction between the basement membrane and mesenchymal cells. We suggest that TM inhibits odontoblast differentiation by causing alterations in the basement membrane which prevent the necessary cell-matrix interaction required for odontoblast differentiation.


Sign in / Sign up

Export Citation Format

Share Document