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At least 55 records · Page 3Linked to original sources
PubMed1972

The effect of phenytoin on the absorption of synthetic folic acid polyglutamate.

The absorption of synthetic pteroyltriglutamate has been measured in nine normal students with and without the anticonvulsant drug phenytoin. It has been shown that phenytoin has no effect on the absorption of this folate polyglutamate. The reasons are discussed for the disparity between this result and those reported in the literature when folate polyglutamates derived from yeast were used.

Adult↗
PubMed1986

Novel macrophage receptor for glucose-modified proteins is distinct from previously described scavenger receptors.

A high-affinity macrophage receptor has been identified that recognizes proteins modified by a common in vivo process, long-term nonenzymatic reaction of glucose with proteins (AGE proteins). This receptor for glucose-modified proteins is now shown to be distinct from previously described scavenger receptors, using competition and crosscompetition experiments between AGE-modified protein and a variety of in vitro-modified scavenger receptor ligands, including unmodified BSA, unmodified low-density lipoproteins (LDL), acetyl-LDL, maleyl-BSA, and formaldehyde-treated BSA. Furthermore, the specific pattern of AGE-protein receptor inhibition by the polyanionic compounds polyinosinic acid, polyadenylic acid, polyglutamic acid, polycytidylic acid, fucoidin, and heparin was distinctly different from that of acetyl-LDL. By thus selectively recognizing a time-dependent in vivo protein modification, macrophages may preferentially degrade senescent macromolecules, thereby having an important role in the regulation of extracellular protein turnover.

Aging↗
PubMed2002

Polyanions decelerate the kinetics of positively charged gramicidin channels as shown by sensitized photoinactivation.

The effects of different anionic polymers on the kinetic properties of ionic channels formed by neutral gramicidin A (gA) and its positively charged analogs gramicidin-tris(2-aminoethyl)amine (gram-TAEA) and gramicidin-ethylenediamine (gram-EDA) in a bilayer lipid membrane were studied using a method of sensitized photoinactivation. The addition of Konig's polyanion caused substantial deceleration of the photoinactivation kinetics of gram-TAEA channels, which expose three positive charges to the aqueous phase at both sides of the membrane. In contrast, channels formed of gram-EDA, which exposes one positive charge, and neutral gA channels were insensitive to Konig's polyanion. The effect strongly depended on the nature of the polyanion added, namely: DNA, RNA, polyacrylic acid, and polyglutamic acid were inactive, whereas modified polyacrylic acid induced deceleration of the channel kinetics at high concentrations. In addition, DNA was able to prevent the action of Konig's polyanion. In single-channel experiments, the addition of Konig's polyanion resulted in the appearance of long-lived gram-TAEA channels. The deceleration of the gram-TAEA channel kinetics was ascribed to electrostatic interaction of the polyanion with gram-TAEA that reduces the mobility of gram-TAEA monomers and dimers in the membrane via clustering of channels.

Acrylic Resins↗
PubMed2006

Characterization of gamma-glutamyl hydrolase produced by Bacillus sp. isolated from Thai Thua-nao.

Gamma-glutamyl hydrolase with a molecular mass of 28 kDa was purified from the culture broth of Bacillus sp. isolated from Thai Thua-nao, a natto-like fermented soybean food. The purified enzyme hydrolyzed chemically synthesized oligo-gamma-L-glutamates but not oligo-gamma-D-glutamates and degraded gamma-polyglutamic acid to a hydrolyzed product of only about 20 kDa (with D- and L-glutamic acid in a ratio of 70:30), suggesting that the enzyme is a gamma-glutamyl hydrolase that cleaves the gamma-glutamyl linkage between L- and L-glutamic acid of gamma-polyglutamic acid.

Bacillus↗
PubMed2000

Role of anionic proteins in kidney stone formation: interaction between model anionic polypeptides and calcium oxalate crystals.

PURPOSE: We tested the effect of molecular weight and amino acid composition (aspartate versus glutamate) in model peptides on calcium oxalate dihydrate (COD) formation to understand how known urinary inhibitor proteins might control spontaneous crystallization. MATERIALS AND METHODS: Supersaturated solutions of CaCl2 and Na2C2O4 in HEPES buffered saline solution were prepared at various calcium (Ca) to oxalate (Ox) ratios, but constant supersaturation, in the presence of protein inhibitors (polyaspartic acid molecular weight series or polyglutamic acid). The resulting crystals were collected and evaluated with optical microscopy. RESULTS: With no added inhibitors, the crystal size increased with Ca to Ox ratio, while the number of crystals decreased. With protein inhibitors at equivalent mass concentrations, intermediate molecular weight proteins produced a greater proportion of COD in Ca rich conditions than did either extreme. In Ox rich conditions, the proportion of COD was directly related to protein molecular weight. However, at equivalent molar concentrations, the proportion of COD produced was directly related to molecular weight under all conditions. Larger protein concentrations were required to produce COD at high Ox conditions, in proportion to the increased number of crystals produced. Polyglutamic acid had a much weaker effect on crystal structure, but it changed the COM morphology. CONCLUSIONS: The results suggest that a discrete number of protein molecules per crystal were required to direct crystallization toward COD, and that a characteristic size of polypeptide chain can be defined. The charge of the side group was not the sole determinant of this effect, as polyglutamic and polyaspartic acids behaved differently. Calcium oxalate crystal nucleation rates appeared to increase with Ox content.

Calcium Oxalate↗
PubMed1981

Nucleosomes will not form on double-stranded RNa or over poly(dA).poly(dT) tracts in recombinant DNA.

We have been unable to "force" double-stranded RNA to fold into nucleosome-like structures using several different histone-RNA "reconstitution" procedures. Even if the histones are first stabilized in octameric form by dimethylsuberimidate cross-linking they are still unable to form specific complexes with the RNA. Moreover double-stranded RNA is unable to induce histones to assemble into octamers although we confirm that the non-nucleic acid homopolymer, polyglutamic acid, has this ability. We have also determined, using pyrimidine tract analysis, that nucleosomes will not form over a sufficiently long segment of poly(dA).poly(dT) in a recombinant DNA molecule. Thus nucleosomes cannot fold DNA containing an 80 base pair poly(dA).poly(dT) segment but a 20 base pair segment can be accommodated in nucleosomes fairly well. Segments of intermediate length can be accommodated but are clearly selected against. Poly(dA).poly(dT) differs only slightly from natural DNA in helix structure. Therefore either this homopolymer resists folding, or nucleosomes are very exacting in the nucleic acid steroid parameters they will tolerate. Such constraints may be relevant to nucleosome positioning in chromatin.

Animals↗
PubMed1973

Stimulation of Sendai virion transcriptase by polyanions.

Exogenous polyribonucleotides stimulated the ribonucleic acid (RNA) transcriptase in Sendai virions. Added yeast RNA, polyadenylic acid, or polycytidylic acid increased incorporation of (3)H-guanosine monophosphate as much as fivefold. The products of stimulated reactions were virus-specific as determined by hybridization with Sendai virion RNA, but they sedimented more slowly (13s) than the product of an unstimulated reaction (16s). The stimulating activity was nondialyzable and heat stable, but was abolished by alkaline hydrolysis. Nucleoside monophosphates, individually or in combination, were ineffective, confirming the requirement for a polymer. Among other substances tested for effects on Sendai virion transcriptase, polyaspartic acid and polyglutamic acid stimulated the enzyme; polyinosinic acid, polyuridylic acid, and polyamines had no effect; and dextran sulfate and polyvinyl sulfate were inhibitory.

Animals↗
PubMed1985

In vitro and in vivo studies of drug-releasing poly(amino acids).

Preliminary efforts directed toward the synthesis and characterization of steroid-polyamino acid conjugates indicate that the preparation of these systems is feasible. Studies have indicated that the steroids may be released from the macromolecule resulting in long-term controlled release systems. Table 4 lists several of the variables that are important in controlling biocompatibility, biodegradation, and drug release characteristics. The biocompatibility, biodegradation, and drug release characteristics are all important in the design and preparation of a drug-polyamino acid delivery system. The variables listed in Table 4 may interact and interrelate to varying degrees when considering each of these factors independently. Although perhaps preliminary, efforts to date indicate that steroids bound to polyglutamic acid or polyglutamic acid derivatives are biocompatible, capable of undergoing biodegradation, and can release drugs at appropriate rates for extended periods of time.

Animals↗
PubMed1999

Dissolution of synthetic hydroxyapatite in the presence of acidic polypeptides.

This article deals with the effect of two acidic polypeptides [polyaspartic acid (PA) and polyglutamic acid (PG)] onto hydroxyapatite (HAP) dissolution by separately considering their influence when they are present only at the HAP interface and when they are both adsorbed and present in the bulk solution. We first determined the amount of adsorbed PA and PG at pH 7.0 and 5.0 onto 10 mg of HAP. Dissolution experiments were performed at pH 5.0 under pH stat conditions by continuously following the consumed protons and released calcium versus time with the aid of specific electrodes. The released phosphate ions were determined by spectrophotometric analysis. The data show that, because of their calcium chelating properties, the polypeptides act as a driving force for HAP dissolution when PA and PG remain present in solution and the interfacial beneficial effect of the adsorbed peptides is erased by the chelating properties of PA and PG present in the solution. When the polypeptides are only adsorbed at the interface, even if a partial PA or PG desorption occurs, HAP dissolution inhibition is still observed.

Adsorption↗