Siberian Ginseng Extract

Key Words: American Ginseng Extract

[Latin Name]  Acanthopanax senticosus (Rupr. Maxim.) Harms

[Specification] Eleuthroside ≧0.8%

[Appearance] Light yellow powder

Plant Part Used: Root

[Particle size] 80Mesh

[Loss on drying] ≤5.0%

[Heavy Metal] ≤10PPM

[Storage] Store in cool & dry area, keep away from the direct light and heat.

[Shelf life] 24 Months

[Package] Packed in paper-drums and two plastic-bags inside.

[Net weight] 25kgs/drum

[What is Siberian Ginseng?]

Eleutherococcus, also known as eleuthero or Siberian ginseng, grows in mountain forests and is native to eastern Asia including China, Japan, and Russia. Traditional Chinese Medicine has used eleutherococcus for reducing lethargy, fatigue, and low stamina as well as increasing endurance and resilience to environmental stresses. Eleutherococcus is considered an “adaptogen,” a term that describes herbs or other substances that, when ingested, appears to help an organism increase resistance to stress. There is strong evidenceEleutherococcus senticosus increases endurance and mental performance in patients with mild fatigue and weakness.

[Benefits]

Eleutherococcus senticosus is a pretty awesome plant and has a lot more benefits that just the graphic above highlights. Here are some of the ones worth mentioning.

1. Energy
2. Focus
3. Anti-Anxiety
4. Anti-Fatigue
5. Chronic Fatigue Syndrome
6. Common Colds
7. Immune Booster
8. Liver Detox
9. Cancer
10. Antiviral
11. High Blood Pressure
12. Insomnia
13. Bronchitis

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1. Contact me at kgahern@davincipress.com / Friend me on Facebook (kevin.g.ahern)
2. Download my free biochemistry book at https://biochem.science.oregonstate.edu/biochemistry-free-and-easy
3. Take my free iTunes U course at https://itunes.apple.com/us/course/biochemistry/id556410409
4. Check out my free book for pre-meds at https://biochem.science.oregonstate.edu/biochemistry-free-and-easy
5. Lecturio videos for medical students – https://www.lecturio.com/medical-courses/biochemistry.course
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Carbohydrates Lecture II Highlights
1.Linking together of more than one sugar residues creates higher order saccharides – disaccharides, trisaccharides, oligosaccharides, and polysaccharides.
2. Most of the linkages in higher order saccharides involve glycosidic bonds.
3. Disaccharides include sucrose, lactose, and maltose.
4. Sucrose is a non-reducing sugar, whereas lactose is a reducing sugar.
5. Oligosaccharides are components of glycoproteins.
6. The most common polysaccharides include glycogen, cellulose, starch, chitin.
7. Polysaccharides can be homopolymers or heteropolymers. Homopolymers include glycogen, cellulose, amylose, amylopectin, and chitin.
8. Glycogen is an animal energy storage polysaccharide, amylopectin and amylose combine to form starch, which is a plant energy storage polysaccharide, cellulose is a plant structural polysaccharide, and chitin is a component of insect exoskeletons.
9. The enzyme cellulase is required to digest the beta 1-4 bonds of cellulose. Ruminants and ungulates contain the bacterium that makes that enzyme.
10. Glycosaminoglycans are polysaccharides that contain either N-acetylgalactosamine or N-acetylglucosamine. They are polyanionic and have interesting chemical properties. Examples include chondroitin sulfates and keratan sulfates of connective tissue, dermatan sulfates, heparin, hyaluronic acid, and others.
11. Proteoglycans are complexes of proteins and glycosaminoglycans that form feathery structures.
12. Glycoproteins consist of a protein linked to an oligosaccharide, usually via an ‘N’ or an ‘O’ linkage. N linkages occur through asparagine of the protein. O linkages occur across serine or threonine of the protein.
13. Oligosaccharides on proteins and lipids have functions in cellular identity and can be recognized and bound by immunoglobulins.
14. Oligosaccharides on the surface of cells help give them their identity. A,B, and O blood group antigens give rise to the various blood types and these arise from carbohydrates on their cell surfaces.
15. Transplanted organs suffer rejection when the new organ has a different oligosaccharide pattern than the organ the recipient originally had. This encourages the immune system to attack it as foreign.
16. All N-linked glycoproteins have the same core of five carbohydrate residues.
17. N-linked glycoproteins have glycosylation (addition of carbohydrate residues) occurring in the endoplamic reticulum and Golgi complex of the cell. O-linked glycoproteins have glycosylation occuring only in the Golgi complex.
18. Movement of modified proteins from the endoplasmic reticulum to the Golgi complex allows for additional carbohydrate modifications to occur, followed by targeting to 1) the cell membrane, 2) release from the cell, or 3) the lysosome.
19. Two terms that you should be aware of are Haworth structures and Fischer projections. Haworth structures refer to the ring forms of sugars. The straight chain forms are referred to as Fischer projections.
20. Oligosaccharides destined to be linked to proteins to make glycoproteins are “built” on dolichol phosphate on the outer portion of the endoplasmic reticulum and then this “flips” to the inside for attachment.
21. Specific carbohydrate residues on the surface glycoproteins of blood cells are binding targets for hemagluttanin proteins on the surface of flu viruses. To exit a cell, the virus must cleave the sialic acid off with a neuraminidase enzyme. Anti-flu drugs like tamiflu act by inhibiting the action of the neuraminidase.

Signaling Highlights
1. Signaling is essential for cells in multicellular organisms to communicate with each other.
2. To do so, cells use first messengers (usually hormones), such as epinephrine (adrenalin), insulin, or epidermal growth factor.
3. Upon binding to a specific receptor on a target cell, the first messenger elicits a response that results in production of a second messenger inside of the target cell. Second messengers include cAMP, cGMP, calcium, diacylglycerol, PIP3, and others.