scholarly journals Cinnamomin, a type II ribosome-inactivating protein, is a storage protein in the seed of the camphor tree (Cinnamomum camphora)

2002 ◽  
Vol 362 (3) ◽  
pp. 659 ◽  
Author(s):  
Ren-shui LIU ◽  
Guo-qing WEI ◽  
Qiang YANG ◽  
Wen-jun HE ◽  
Wang-Yi LIU
Keyword(s):  
Storage Protein ◽  
Cinnamomum Camphora ◽  
Type Ii ◽  
Ribosome Inactivating Protein ◽  
Camphor Tree

Cinnamomin, a type II ribosome-inactivating protein, is a storage protein in the seed of the camphor tree (Cinnamomum camphora)

2002 ◽  
Vol 362 (3) ◽  
pp. 659-663 ◽  
Author(s):  
Ren-shui LIU ◽  
Guo-qing WEI ◽  
Qiang YANG ◽  
Wen-jun HE ◽  
Wang-Yi LIU
Keyword(s):  
Western Blotting ◽  
Storage Protein ◽  
Storage Proteins ◽  
Protein Body ◽  
Physiological Role ◽  
Seed Storage Proteins ◽  
Cinnamomum Camphora ◽  
Type Ii ◽  
Ribosome Inactivating Protein ◽  
Camphor Tree

Cinnamomin is a novel type II ribosome-inactivating protein (RIP) isolated in our laboratory from the seed of the camphor tree (Cinnamomum camphora). In this paper the physiological role it plays in the plant cell was studied. Northern and Western blotting revealed that cinnamomin was expressed specifically in cotyledons. It accumulated in large amounts simultaneously with other proteins at the post-stages of seed development. Cinnamomin degraded rapidly during the early stages of seed germination. Endopeptidase was proved to play an important role in the degradation of cinnamomin. Western blotting of total proteins from the protein body with antibodies against cinnamomin demonstrated that it only existed in this specific cellular organelle as a storage protein. The similar properties of cinnamomin and other seed storage proteins of dicotyledons were compared. We conclude that cinnamomin is a special storage protein in the seed of C. camphora.

Structural and functional studies of cinnamomin, a new type II ribosome-inactivating protein isolated from the seeds of the camphor tree

2001 ◽  
Vol 268 (22) ◽  
pp. 5723-5733 ◽  
Author(s):  
Liang Xie ◽  
Bao-Zhong Wang ◽  
Rong-gui Hu ◽  
Hong-bin Ji ◽  
Li Zhang ◽  
...  
Keyword(s):  
Type Ii ◽  
Ribosome Inactivating Protein ◽  
Functional Studies ◽  
New Type ◽  
Camphor Tree

2.8-Å crystal structure of a nontoxic type-II ribosome-inactivating protein, ebulin l

2001 ◽  
Vol 43 (3) ◽  
pp. 319-326 ◽  
Author(s):  
John M. Pascal ◽  
Philip J. Day ◽  
Arthur F. Monzingo ◽  
Stephen R. Ernst ◽  
Jon D. Robertus ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Type Ii ◽  
Ribosome Inactivating Protein

The same nuclear proteins bind to the 5?-flanking regions of genes for the rice seed storage protein: 16 kDa albumin, 13 kDa prolamin and type II glutelin

1996 ◽  
Vol 32 (4) ◽  
pp. 621-630 ◽  
Author(s):  
Masayuki Nakase ◽  
Takehisa Yamada ◽  
Takahiro Kira ◽  
Junji Yamaguchi ◽  
Naohito Aoki ◽  
...  
Keyword(s):  
Storage Protein ◽  
Seed Storage Protein ◽  
Seed Storage ◽  
Nuclear Proteins ◽  
Rice Seed ◽  
Type Ii ◽  
Flanking Regions

scholarly journals Crystallization and preliminary X-ray studies of a galactose-specific lectin from the seeds of bitter gourd (Momordica charantia)

2010 ◽  
Vol 66 (9) ◽  
pp. 1037-1040 ◽  
Author(s):  
Thyageshwar Chandran ◽  
Alok Sharma ◽  
M. Vijayan
Keyword(s):  
Structural Investigation ◽  
Structural Information ◽  
Disulfide Bridge ◽  
Momordica Charantia ◽  
Bitter Gourd ◽  
Molecular Replacement ◽  
Type Ii ◽  
Ribosome Inactivating Protein ◽  
X Ray ◽  
Chain Type

A galactose-specific lectin from the seeds of bitter gourd (Momordica charantia) is a four-chain type II ribosome-inactivating protein (RIP) resulting from covalent association through a disulfide bridge between two identical copies of a two-chain unit. The available structural information on such four-chain RIPs is meagre. The bitter gourd lectin was therefore crystallized for structural investigation and the crystals have been characterized. It is anticipated that the structure of the orthorhombic crystals will be analysed using molecular replacement by taking advantage of its sequence, and presumably structural, homology to normal two-chain type II RIPs.

scholarly journals Essential oils of camphor tree (cinnamomum camphora nees & eberm) cultivated in Southern Brazil

2000 ◽  
Vol 43 (3) ◽  
pp. 313-316 ◽  
Author(s):  
Caren D. Frizzo ◽  
Ana C. Santos ◽  
Natalia Paroul ◽  
Luciana A. Serafini ◽  
Eduardo Dellacassa ◽  
...  
Keyword(s):  
Essential Oils ◽  
Methyl Silicone ◽  
Cinnamomum Camphora ◽  
Southern Brazil ◽  
Main Components ◽  
Retention Indexes ◽  
Camphor Tree

The essential oils of two varieties of Camphor tree (Cinnamomum camphora Nees & Eberm, Lauraceae), known as Hon-Sho and Ho-Sho cultivated in experimental stands in Southern Brazil were studied. The essential oils were obtained from the leaves and twigs of young plants by hydrodistillation. The identification of the components was performed using GC, GC/MS and retention indexes on methyl silicone and carbowax phases. The main components identified were linalool in the Ho-Sho and camphor in the Hon-Sho.

Cinnamomin—a Versatile Type II Ribosome-inactivating Protein

2004 ◽  
Vol 36 (3) ◽  
pp. 169-176 ◽  
Author(s):  
Hong Xu ◽  
Wang-Yi Liu
Keyword(s):  
Theoretical Study ◽  
Physiological Role ◽  
Type Ii ◽  
Insect Larvae ◽  
Ribosome Inactivating Protein ◽  
Ribosome Inactivating Proteins ◽  
Enzymatic Mechanism ◽  
Potential Applications ◽  
And Function ◽  
Mature Seeds

Abstract Ribosome-inactivating proteins (RIPs) are a group of toxic proteins that can specifically act on the universally conserved sarcin/ricin domain (S/R domain) of the largest RNA in ribosome and thus irreversibly inactivate ribosome for protein synthesis. Cinnamomin is a multifunctional type II RIP isolated in our laboratory from the mature seeds of the camphor tree. This protein has been extensively studied with regard to its purification, characteristics, structure and function, genetic expression, enzymatic mechanism, physiological role in seed cell and toxicity to cancer cells and insect larvae. The research results of cinnamomin obtained in our laboratory are summarized in this review. Understanding of cinnamomin and the relative new proteins will help expand our knowledge of RIPs and may accelerate theoretical study and the development of their potential applications.

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