scholarly journals Identification of the 7S and 11S globulins as percutaneously sensitizing soybean allergens as demonstrated through epidermal application of crude soybean extract

2018 ◽  
Vol 82 (8) ◽  
pp. 1408-1416 ◽  
Author(s):  
Hiroki Murakami ◽  
Takashi Ogawa ◽  
Akiho Takafuta ◽  
Erika Yano ◽  
Nobuhiro Zaima ◽  
...  
1990 ◽  
Vol 38 (1) ◽  
pp. 92-95 ◽  
Author(s):  
V. V. Suchkov ◽  
I. A. Popello ◽  
V. Ya. Grinberg ◽  
V. B. Tolstoguzov

Molecules ◽  
2019 ◽  
Vol 24 (6) ◽  
pp. 1082 ◽  
Author(s):  
Seham Abdel-Shafi ◽  
Abdul-Raouf Al-Mohammadi ◽  
Ali Osman ◽  
Gamal Enan ◽  
Samar Abdel-Hameid ◽  
...  

The present work was carried out to determine the characteristics and antibacterial activity of 7S and 11S globulins isolated from cowpea seed (Vigna unguiculata (L.) Walp.). The molecular mass of 7S globulin was demonstrated by SDS-PAGE bands to be of about 132, 129 and 95 kDa corresponding the α/, α and β subunits. The molecular mass of 11S globulin was demonstrated by SDS-PAGE bands to be existed between 28 and 52 kDa corresponding the basic and acidic subunits. The minimum inhibitory concentrations MICs of 7S and 11S globulins isolated from cowpea seed were determined against Gram positive bacteria viz: Listeria monocytogenes LMG 10470, Listeria ivanovii FLB 12, Staphylococcus aureus ATCC 25923 and Streptococcus pyogenes ATCC 19615, and Gram negative bacteria such as Klebsiella pneumonia ATCC 43816, Pseudomonas aeruginosa ATCC 26853, Escherichia coli ATCC 25922 and Salmonella ATCC 14028 using disc diffusion assay; they were showed to be in the range 10 to 200 µg/mL. Transmission electron microscope (TEM) examination of the protein-treated bacteria showed the antibacterial action of 11S globulin against S. typhimurium and P. aeruginosa was manifested by signs of cellular deformation, partial and complete lysis of cell components. Adding 11S globulin at both concentrations 50 and 100 µg/g to minced meat showed considerable decreases in bacterial counts of viable bacteria, psychrotrophs and coliforms compared to controls during 15 days storage at 4 °C, reflecting a promising perspective to use such globulin as a meat bio-preservative.


1983 ◽  
Vol 47 (6) ◽  
pp. 1229-1237 ◽  
Author(s):  
Tatsunori YAMAGISHI ◽  
Atsuko MIYAKAWA ◽  
Naotaka NODA ◽  
Fumio YAMAUCHI

2012 ◽  
Vol 93 (7) ◽  
pp. 1687-1691 ◽  
Author(s):  
Jun Chen ◽  
Xiangyan Chen ◽  
Qingjun Zhu ◽  
Fengliang Chen ◽  
Xiaoyan Zhao ◽  
...  

2016 ◽  
Vol 14 (2) ◽  
pp. 163-167
Author(s):  
V. G. Adamovskaya ◽  
O. O. Molodchenkova ◽  
V. I. Sichkar ◽  
T. V. Kartuzova ◽  
L. Y. Bezkrovnaya ◽  
...  

Aims. The goal of research was to study a character of changes and relationship between level of 7S and 11S globulins, their ratio and protein content  in the soybean seed of F6-F8 hybrid lines and their parental forms of different genetic origin in the connection of protein quality breeding. Methods. 7S and 11S globulins were isolated by method, which was developed in the Laboratory of Plant Biochemistry (Patent # 42181). Results. The features of 7S and 11S globulins content and their ratio in the soybean seed of F6 -F8 hybrid lines and their parental forms of different genetic origin were identified. It was established, that varieties and hybrid lines are characterized by considerable distinctions of 7S and 11S globulins contents and their ratio in the soybean protein. A connection between 7S and 11S globulins levels and protein content in the seed of soybean F6- F8 hybrid lines wasn’t established. Conclusions. It was elucidated that the growth conditions influence on the protein content, 11S and 7S globulins level, their ratio and relationship between these parameters in the soybean seeds of F6-F8 hybrid lines and their parental forms of different genetic origin, so that have to be introduced in the selection program of  soybean genotypes  of food direction soybean breeding as these parameters connected with the   food nutritional quality.Key words: Glicine max L., protein, 11S globulin, 7S globulin.


1986 ◽  
Vol 50 (10) ◽  
pp. 2429-2435
Author(s):  
Takashi Nakamura ◽  
Shigeru Utsumi ◽  
Tomohiko Mori

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