نتایج جستجو برای: glutelin

تعداد نتایج: 191  

Journal: :Plant physiology 1986
H B Krishnan T W Okita

When the glutelin protein fraction of rice (Oryza sativa L.) seeds was fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, three size classes of proteins, 51 kilodaltons (kD), 34 to 37 kD, and 21 to 22 kD, as well as a contaminating prolamine polypeptide of 14 kD were detected. Antibodies were raised against these proteins and employed in studies to determine whether a pr...

Journal: :Rice 2021

Abstract Background Rice is not only an essential food but also a source of high quality protein. Polyploidy evolutionary trajectory in plants, and enhancing glutelin by polyploidization attractive strategy for improving the nutritional value rice seeds presents great potential commercial rice. Elucidating mechanisms underlying synthesis accumulation tetraploid significance. Results To enhance ...

2017
Fumie Takaiwa

The major seed storage protein of rice (Oryza sativa L.), glutelin, is encoded by a smal1 multigene family of about 10 copies per haploid genome. Eight genes have a)ready been sequenced at both the cDNA and genomic DNA levels (Takaiwa et al. 1987a, b, 1989, 1991a, c, Okita et al, 1989), All the glutelin genes are specifically expressed in the maturing seed (Okita et al. 1989, Takaiwa et al. 199...

Journal: :Plant physiology 2002
Yoko Takemoto Sean J Coughlan Thomas W Okita Hikaru Satoh Masahiro Ogawa Toshihiro Kumamaru

Rice (Oryza sativa) accumulates prolamins and glutelins as storage proteins. The latter storage protein is synthesized on the endoplasmic reticulum (ER) as a 57-kD proglutelin precursor, which is then processed into acidic and basic subunits in the protein storage vacuole. Three esp2 mutants, CM1787, EM44, and EM747, contain larger amounts of the 57-kD polypeptide and corresponding lower levels...

Journal: :Journal of environmental biology 2011
Reema Srivastava Bijoy K Roy

The isolation procedure of the seed proteins of Amaranthus blitum have been analyzed at different pH conditions. Qualitative studies were carried out by using electrophoretic technique sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Mainly four protein fractions i.e. albumin, globulin, prolamin and glutelin were obtained. Protein isolates were prepared by (a) extraction a...

2016
Kyoungwon Cho Hye-Jung Lee Yeong-Min Jo Sun-Hyung Lim Randeep Rakwal Jong-Yeol Lee Young-Mi Kim

Seed storage proteins (SSPs) such as glutelin, prolamin, and globulin are abundant components in some of the most widely consumed food cereals in the world. Synthesized in the rough endoplasmic reticulum (ER), SSPs are translocated to the protein bodies. Prolamins are located at the spherical protein body I derived from the ER, whereas, glutelins and globulin are accumulated in the irregularly ...

2013
Ma T. Espino‐Sevilla Maria E. Jaramillo‐Flores Rodolfo Hernández‐Gutiérrez Juan C. Mateos‐Díaz Hugo Espinosa‐Andrews Ana P. Barba de la Rosa Jose O. Rodiles‐López Socorro Villanueva‐Rodríguez Eugenia C. Lugo‐Cervantes

Ditaxis heterantha is a plant of the Euphorbiaceae family that grows in semiarid regions of Mexico. It produces yellow pigmented seeds that are used for coloring of foods. The seeds contain about 20% of proteins. Proteins of D. heterantha were extracted and fractionated on the basis of solubility. Three main protein fractions were obtained: glutelins, 488 ± 0.5; albumins, 229 ± 2; and total glo...

Journal: :Plant foods for human nutrition 2008
Kyungjin Lee Kiyoon Kang Munyoung Park Young-Min Woo Kyoungwhan Back

Serotonin N-hydroxycinnamoyltransferase (SHT) is a key enzyme in the synthesis of feruloylserotonin (FS) and 4-coumaroylserotonin (CS). These serotonin derivatives show strong antioxidant activity, making them valuable for both nutritional and pharmacological use in humans. Ectopic expression of SHT under the control of the endosperm specific-glutelin and prolamin promoters from rice was produc...

Journal: :The Journal of biological chemistry 1987
K Abe Y Emori H Kondo K Suzuki S Arai

A cDNA clone for a cysteine proteinase inhibitor of rice (oryzacystatin) was isolated from a lambda gt10 cDNA library of rice immature seeds by screening with synthesized oligonucleotide probes based on partial amino acid sequences of oryzacystatin. A nearly full-length cDNA clone was obtained which encoded 102-amino acid residues. The amino acid sequence of oryzacystatin deduced from the cDNA ...

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