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GST 29AABCS6715J1Z2

Unusual Amino Acids

S-Acetyl-L-Glutathione

S-Acetyl-L-Glutathione

Glutathione is a tripeptide comprised of three amino acids (cysteine, glutamic acid, and glycine) present in most mammalian tissue. Glutathione acts as an antioxidant, a free radical scavenger and a detoxifying agent. Glutathione is also important as a cofactor for the enzyme glutathione peroxidase, in the uptake of amino acids, and in the synthesis of leukotrienes. Certificate of Analysis (COA) & MSDS are available.

Uses:  Ingredient in baked goods and baking mixes, beverages and beverages bases, breakfast cereals, cheeses, chewing gum, coffee and tea, condiments and relishes, dairy product analogs, gelatins, puddings and fillings, grain products and pastas, gravies and sauces, hard candy, milk products, plant protein products, processed fruits and fruit juices, processed vegetables and vegetables juices, salty snacks, soft candy, soups and soup mixes, and sugar substitutes, at levels ranging from 5 to 742.5 milligrams per serving
Hazard Classes and Categories:

Skin Irrit. 2 (20%)
Eye Dam. 1 (20%)

STOT SE 3 (20%)

Muta. 2 (90%)


Biosynthesis and occurrence:Glutathione biosynthesis involves two adenosine triphosphate-dependent steps:First, gamma-glutamylcysteine is synthesized from L-glutamate and cysteine. This conversion requires the enzyme glutamate–cysteine ligase (GCL, glutamate cysteine synthase). This reaction is the rate-limiting step in glutathione synthesis. Second, glycine is added to the C-terminal of gamma-glutamylcysteine. This condensation is catalyzed by glutathione synthetase.While all animal cells are capable of synthesizing glutathione, glutathione synthesis in the liver has been shown to be essential. GCLC knockout mice die within a month of birth due to the absence of hepatic GSH synthesis.The unusual gamma amide linkage in glutathione protects it from hydrolysis by peptidases.

Biochemical function: Glutathione exists in reduced (GSH) and oxidized (GSSG) states. The ratio of reduced glutathione to oxidized glutathione within cells is a measure of cellular oxidative stress where increased GSSG-to-GSH ratio is indicative of greater oxidative stress. In healthy cells and tissue, more than 90% of the total glutathione pool is in the reduced form (GSH), with the remainder in the disulfide form (GSSG).In the reduced state, the thiol group of cysteinyl residue is a source of one reducing equivalent. Glutathione disulfide (GSSG) is thereby generated. The oxidized state is converted to the reduced state by NADPH. This conversion is catalyzed by glutathione reductase:
NADPH + GSSG + H2O → 2 GSH + NADP+ + OH−

Bioavailability and supplementation: Systemic bioavailability of orally consumed glutathione is poor because the tripeptide is the substrate of proteases (peptidases) of the alimentary canal, and due to the absence of a specific carrier of glutathione at the level of cell membrane.Because direct supplementation of glutathione is not successful, supply of the raw nutritional materials used to generate GSH, such as cysteine and glycine, may be more effective at increasing glutathione levels. Other antioxidants such as ascorbic acid (vitamin C) may also work synergistically with glutathione, preventing depletion of either. The glutathione-ascorbate cycle, which works to detoxify hydrogen peroxide (H2O2), is one very specific example of this phenomenon.
Low glutathione is commonly observed in wasting and negative nitrogen balance, as seen in cancer, HIV/AIDS, sepsis, trauma, burns, and athletic overtraining. Low levels are also observed in periods of starvation. These effects are hypothesized to be influenced by the higher glycolytic activity associated with cachexia, which result from reduced levels of oxidative phosphorylation.

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    Harsha M. C.

    (Managing Director)

    Siddhi Vinayaka Spechem Private Limited

    Jayanagar, Bengaluru, Karnataka, India

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