Methionine sulfate

Zinc metharsenite. See Zinc arsenite Zinc methionine sulfate CAS 56329-42-1... 

L-Tyrosine DL-a-Valine L-Valine Wheat (Triticum vulqare) qerm oil Zinc acetate Zinc citrate Zinc gluconate Zinc methionine sulfate Zinc oxide Zinc stearate Zinc sulfate Zinc sulfate heptahydrate dietary supplement, food special dietary use D-Pantothenamide dietary supplement, gelatin capsules Retinyl palmitate... 

Zinc lactate Zinc methionine sulfate Zinc sulfatej Zinc sulfate heptahydrate dietary supplement, powder diet supplements Calcium caseinate... 

Sodium ascorbate Sodium gluconate Sodium pantothenate Sodium phosphate dibasic heptahydrate Thiamine HCI L-Threonine Tocopherol D-a-Tocopherol pL-a-Tocopherol d-a-Tocopheryl acetate dl-a-Tocopheryl acetate DL-a-Valine L-Valine Zinc gluconate Zinc methionine sulfate Zinc sulfate Zinc sulfate heptahydrate nutrient, plant... 

Cupric sulfate pentahydrate nutrient, special dietary food Ferric choline citrate nutrient, special dietary use Aluminum nicotinate nutrient, sweeteners DL-Alanine nutrient, tablets Wheat (Triticum vulgare) germ nutrient, vitamin tablets Ferrous gluconate Ferrous gluconate dihydrate Potassium D-gluconate Zinc gluconate Zinc methionine sulfate nutrient, yeast Ammonium nitrate nutrient, yeast fermentation Ammonium bicarbonate Ammonium phosphate Ammonium phosphate, dibasic nutrient, yeast prod. 

Fig. 10.1. Defects of transmethylation (methioninehomocysteine), transsulfuration (methionine sulfate), and remethylation (homocysteine - methionine) enzymes of sulfur amino acid metabolism 10.1, methionine adenosyltransferase 10.2, cystathionine ) -synthase 10.3, y-cystathionase 10.4, sulfite oxidase 10.5, molybdenum cofactor 10.6, methylenetetrahydrofolate reductase 10.7 and 10.8, methionine synthase.

Limits are listed in Title 21 of the U.S. Code of Federal Regulations for levels of cadmium as an impurity in (1) color additives that are exempt from certification—cadmium must be not more than 15 ppm in bronze powder, copper powder, zinc oxide, and luminescent zinc sulfide and 2) food additives permitted for direct addition to food for human consumption—cadmium must be less 0.1 ppm in baker s yeast protein, not more than 0.05 ppm in zinc methionine sulfate, and less than 0.13 ppm in bakers yeast glycan (FDA 2013a). 

Sulfur deficiency usually is not a problem for mminants because the mminal microflora can utilize sulfur-containing amino acids. A deficiency can occur, however, when an NPN source is fed. L-Methionine [63-68-3] is the most biologically available source of sulfur (21). Various sulfates are intermediate in sulfur avadabiHty, and elemental sulfur is the least available source of sulfur. 

Sulfur. Sulfur is present in every cell in the body, primarily in proteins containing the amino acids methionine, cystine, and cysteine. Inorganic sulfates and sulfides occur in small amounts relative to total body sulfur, but the compounds that contain them are important to metaboHsm (45,46). Sulfur intake is thought to be adequate if protein intake is adequate and sulfur deficiency has not been reported. Common food sources rich in sulfur are Hsted in Table 6. 

Detoxifica.tlon. Detoxification systems in the human body often involve reactions that utilize sulfur-containing compounds. For example, reactions in which sulfate esters of potentially toxic compounds are formed, rendering these less toxic or nontoxic, are common as are acetylation reactions involving acetyl—SCoA (45). Another important compound is. Vadenosylmethionine [29908-03-0] (SAM), the active form of methionine. SAM acts as a methylating agent, eg, in detoxification reactions such as the methylation of pyridine derivatives, and in the formation of choline (qv), creatine [60-27-5] carnitine [461-06-3] and epinephrine [329-65-7] (50). 

Phethenylate sodium Ammonium chloride Cyclofenil Methionine Ammonium sulfate Aminobenzoic acid Fibrinolysin Ammonium sulfamate Cyclamate calcium Ammonium thiocyanate Acetazolamide Clonidine HCl Tolonidine nitrate 2oxazo lamina d-Amphetamine Tanphetamin Ampicillin Mezlocillin Talampicillin... 

The second important issue related to commercial use of desulfurization biocatalysts is their inhibition by sulfate. The sulfur repression mechanism in most Rhodococcus species limits their use or activity in presence of sulfate- and sulfur-containing amino-acids such as cysteine, methionine, etc. To alleviate this problem, expression of the dsz genes under the control of alternate promoters has been investigated. 

Another report describing an approach to achieve alleviation of sulfur repression came from the Matsui research group. The dsz genes were cloned into a strain Rhodococcus sp. strain T09 under the promoter rrn of the strain T09 using a Rhodococcus-E. coli shuttle vector [214,215], This resulted in a strain which desulfurized DBT to 2-HBP in presence of sulfate, cysteine, or methionine. Similar approach was also used by Kurane to construct a gene expressing dszA-D enzymes, which eliminate the sulfate inhibition effects [216],... 

Lim, C., RH. Klesius, and P.L. Duncan. 1996. Immune response and resistance of channel catfish to Edward-siella ictaluri challenge when fed various dietary levels of zinc methionine and zinc sulfate. Jour. Aquat. Anim. Health 8 302-307. 

The most common posttranslational modifications, discussed in the following sections, include phosphorylation, sulfation, disulfide formation, N-methylation, O-methylation, S-methylation, N-acetylation, hydroxylation, glycosylation, ADP-ribosylation, prenylation, biotinylation, lipoylation, and phosphopan-tetheine tethering. Many of the posttranslational modifications are proven to be cross talks. Other modifications exist in a smaller extent and include oxidation of methionine, C-methylation, ubiquitylation, carboxylation, and amidation. These topics will not be covered in this chapter which is meant to focus primarily on the recent literature (2005-08). For a more complete coverage of all posttranslational modifications and earlier literature (up to 2005), the reader is referred to Professor Christopher T. Walsh s book Posttranslational Modification of Proteins Expanding Nature s Inventory ... 

Not all cytochromes from sulfate-reducing bacteria reduce Fe(III) or other metals. D. vulgaris produces a cyt C553, which has a molecular mass of 9 kDa, midpoint redox potential of OmV, and a single heme and the iron atom is coordinated by histidine methionine. It is unclear at this time if the inability of this cyt C553 to reduce metals is due to lack of a bishistidinyl iron coordination or to some other factor, such as steric hinderance owing to orientation of heme in the protein. 

Protons are mainly derived from two sources—free acids in the diet and sulfur-containing amino acids. Acids taken up with food— e.g., citric acid, ascorbic acid, and phosphoric acid—already release protons in the alkaline pH of the intestinal tract. More important for proton balance, however, are the amino acids methionine and cysteine, which arise from protein degradation in the cells. Their S atoms are oxidized in the liver to form sulfuric acid, which supplies protons by dissociation into sulfate. 

For the sulfation of peptides that do not contain methionine residues, the use of protecting groups that are cleaved by hydrogenolysis represents, independent of the sulfation procedure followed, the safest approach (see Scheme 7)J52,96"... 

Ethanedithiol is added in the sulfating step to prevent oxidation of the methionine residues and in the deprotection step with TBAF to quench the dibenzofulvene, although thiol groups are expected to be sulfated at higher rates than phenolic groups. 

The mild acidolytic cleavage procedure noted above is used to deprotect various side chain protected peptides synthesized in solution or on chlorotrityl-resin with tyrosine O-sulfate synthons as listed in Table 4. The overall yields are significantly superior to those obtained by postsynthetic sulfation of the purified peptides, since they are typical for synthetic peptides after the final deprotection and purification step. The additional main advantage of this approach derives from a facile analytical characterization, since sulfonated byproducts at the tyrosine and tryptophan level, as well as oxidation of the methionine residues resulting from postsynthetic sulfation of tyrosine peptides are avoided. 

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