Protein polyglutamate

Whey proteins have been purified on a hydroxyapatite support using EGTA (ethylene glycol bis( /3-aminoethylether)-N, N, N, N tetraacetic acid) and PGA (polyglutamic acid) as displacers.48... 

The purified E. coli protein has a molecular weight of 49 kD. It does not require any divalent cation for activity. It contains two different noncovalently bound chromophores that absorb light. One chromophore is flavin adenine dinucleotide (FADH- or FADH2). The other is 5,10-methenyltetrahydrofolyl polyglutamate (MTHF). The absorption of light by the chromophores is essential for the enzymatic reversal of the pyrimidine dimer back to the original pyrimidine monomers. However,... 

Haurowitz and Bursa (1949) carried out a study on a number of proteins and the capsular polyglutamic acid of B. anthracis to determine what... 

These methods of the reaction between 9-anthryldiazomethane and carboxylic groups of macromolecules permit to bond LM to side groups of synthetic and natural polymers and copolymers of acrylic and vinylbenzoic acids hydrolyzed copolymers of maleic anhydride , carboxymethylcellulose comb-like alkyl acrylates , polyglutamic acid and other synthetic polypeptides as well as proteins, such as invertase or ribonuclease l... 

Volk, E.L. and Schneider, E. (2003) Wild-type breast cancer resistance protein (BCRP/ABCG2) is a methotrexate polyglutamate transporter. Cancer Research, 63, 5538—5543. 

Surprisingly, a method of antifolate resistance commonly cited in tumor cells is gene amplification resulting in increased target protein and decreased anti-folate efficacy, which has yet to be identified in any clinically relevant isolate. A further difference in antifolate resistance between mammalian cells and the parasitic cell is altered polyglutamation of die antifolate drugs. In mammalian cells, folates are taken up by a folate transport system and once inside the cell are poly-glutamated to trap the folates intracellularly. A reported mechanism of resistance in the cancer cell is the loss of... 

The intensive studies on the genetic code and on the proteins in recent years have led to a fairly good understanding of the mechanism of protein biosynthesis . The biosynthetic mechanism involved in the formation of peptides has not yet been studied in equal detail. Some physiologically active peptides like bradykinin and angiotensin are known to be derived from proteins by a specific enzymatic hydrolysis. Other peptides, like glutathione - , ophthalmic acid , the nucleotide-pentapeptide from Staph, aureus and y-polyglutamic acid have been shown to require for their synthesis only a soluble enzyme system. Their biosynthetic mechanism is therefore entirely different from that of the proteins. Such a different type of mechanism has also been demonstrated lately to be involved in the synthesis of peptide antibiotics. 

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